BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 08-21-2010, 11:45 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,565
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default 1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.

1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.

Related Articles 1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.

Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11881-5

Authors: Cohen RE, Takama M, Schachman HK

The 1H NMR spectrum of the catalytic subunit of Escherichia coli aspartate transcarbamoylase (EC 2.1.3.2) was simplified by using strains auxotrophic for the aromatic amino acids and a growth medium containing fully deuterated Trp, Phe, and His and partially deuterated Tyr. 1H resonances for Tyr in the catalytic trimer (M(r) = 10(5)) were partially resolved into five peaks at 27 degrees C, which above 50 degrees C were further resolved to give a distinct resonance for each of the eight Tyr residues in the polypeptide chain. Experiments on chemically modified catalytic subunits and on a mutant form in which Tyr-165 was converted to Ser-165 led to the assignment of resonances for Tyr-165, Tyr-240, and Tyr-185. Binding of the substrate, carbamoyl phosphate, caused shifts of two of the unassigned resonances, and the subsequent binding of the aspartate analog succinate perturbed the resonances corresponding to Tyr-165 and Tyr-240. The bisubstrate analog N-(phosphonacetyl)-L-aspartate produced a spectrum differing considerably from that caused by the combination of carbamoyl phosphate and succinate. The NMR spectrum for the Tyr-165-->Ser mutant trimer showed clearly that the single amino acid substitution caused conformational changes affecting the environment of residues remote from the position of the replacement. In contrast, the inactive mutant subunit in which Gly-128 was replaced by Asp exhibited a spectrum virtually identical to that of the wild-type protein. However, addition of the substrate carbamoyl phosphate caused a marked change in the spectrum of the mutant enzyme, whereas that of the wild-type trimer was altered only slightly, showing that the effect of the amino acid substitution was manifested in the NMR spectrum only with the liganded enzyme.

PMID: 1465412 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Multidimensional NMR identifies the conformational shift essential for catalytic comp
Multidimensional NMR identifies the conformational shift essential for catalytic competence in the 60-kDa Drosophila melanogaster dUTPase trimer. Related Articles Multidimensional NMR identifies the conformational shift essential for catalytic competence in the 60-kDa Drosophila melanogaster dUTPase trimer. J Biol Chem. 2004 Apr 23;279(17):17945-50 Authors: Dubrovay Z, Gáspári Z, Hunyadi-Gulyás E, Medzihradszky KF, Perczel A, Vértessy BG The catalytic mechanism of dUTP pyrophosphatase (dUTPase), responsible for the prevention of uracil...
nmrlearner Journal club 0 11-24-2010 09:25 PM
[NMR paper] NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Sa
NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Salmonella typhimurium. Related Articles NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Salmonella typhimurium. Biochim Biophys Acta. 2003 Mar 17;1620(1-3):8-14 Authors: Delgoda R, Lian LY, Sandy J, Sim E Arylamine N-acetyltransferases (NAT) are a family of enzymes found in both eucaryotes and procaryotes, which catalyse the N-acetylation of a range of arylamine and hydrazine drugs and carcinogenic arylamines, using acetyl...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues i
Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy. Related Articles Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy. J Am Chem Soc. 2002 May 22;124(20):5714-7 Authors: Tollinger M, Forman-Kay JD, Kay LE A triple-resonance NMR pulse scheme is presented for measuring aspartic and glutamic acid side-chain pK(a) values in unfolded protein states where chemical shift...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-
Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-YIG superfamily member, using NMR restraints and Monte Carlo dynamics. Related Articles Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-YIG superfamily member, using NMR restraints and Monte Carlo dynamics. Protein Eng. 2001 Oct;14(10):717-21 Authors: Bujnicki JM, Rotkiewicz P, Kolinski A, Rychlewski L Using a recent version of the SICHO algorithm for in silico protein folding, we made a blind prediction of the tertiary...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMR paper] NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural inf
NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit. Eur J Biochem. 1996 Oct 1;241(1):229-42 Authors: ...
nmrlearner Journal club 0 08-22-2010 02:20 PM
[NMR paper] FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin.
FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin. Int J Biol Macromol. 1995 Apr;17(2):74-80 Authors: Belton PS, Colquhoun IJ, Grant A, Wellner N, Field JM, Shewry PR, Tatham AS The hydration behaviour of a purified high-M(r) subunit of glutenin has been studied using Fourier transform infra-red (FTIR) and nuclear magnetic...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit
Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands. Related Articles Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands. Biochemistry. 1993 Aug 31;32(34):8782-91 Authors: Kaufman J, Siegel LM, Spicer LD The heme protein subunit of sulfite reductase (SiR-HP; M(r) 64,000) from Escherichia coli as isolated contains the isobacteriochlorin siroheme exchange-coupled to a cluster in the 2+ oxidation state. SiR-HP in the presence of a suitable...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] 31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Esc
31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl. Related Articles 31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl. J Biol Chem. 1991 Apr 15;266(11):6690-2 Authors: Pas HH, Meyer GH, Kruizinga WH, Tamminga KS, van Weeghel RP, Robillard GT The mannitol-specific phosphotransferase system transport protein, Enzyme IIMtl, contains two catalytically important phosphorylated amino acid...
nmrlearner Journal club 0 08-21-2010 11:16 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This Thread:

Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2017, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 03:38 PM.


Map