NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes...
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[NMR paper] NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Related Articles NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Protein Sci. 2016 Jan 8;
Authors: Mohanty B, Geralt M, Wüthrich K, Serrano P
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence...
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01-11-2016 03:57 PM
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes...
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01-09-2016 04:06 PM
[NMR images] You dramatic bitcoin. You dramatic.
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Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Abstract Segmental isotopic labeling is a powerful labeling tool to facilitate NMR studies of larger proteins by not only alleviating the signal overlap problem but also retaining features of uniform isotopic labeling. Although two approaches, expressed protein ligation (EPL) and protein trans-splicing (PTS), have been mainly used for segmental isotopic labeling, there has been no single example in which both approaches have been...
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07-02-2012 06:18 AM
[NMR paper] Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon
Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
Related Articles Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
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NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the c
NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1).
Related Articles NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1).
J Biol Chem. 2010 Nov 12;
Authors: Yokogawa M, Osawa M, Takeuchi K, Mase Y, Shimada I
G protein-activated inwardly rectifying potassium channel (GIRK) plays crucial roles in regulating heart...
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[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...
Dramatic Domain Rearrangements of the CyanobacterialOrange Carotenoid Protein upon Photoactivation
Linear Mode
