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NMR processing:
MDD
NMR assignment:
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MARS
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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:
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RPF scores
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Chemical shifts:
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Vasco
iCing
RDCs:
DC
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Pseudocontact shifts:
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Protein geomtery:
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PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
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ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
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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


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Default Evidence for oxidation-state-dependent conformational changes in human ferredoxin fro

Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.

Related Articles Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.

Biochemistry. 1998 Mar 17;37(11):3965-73

Authors: Xia B, Volkman BF, Markley JL

Human ferredoxin belongs to the vertebrate ferredoxin family which includes bovine adrenodoxin. It is a small (13.8 kDa) acidic protein with a [2Fe-2S] cluster. It functions as an electron shuttle in the cholesterol side-chain cleavage reaction which is the first step of steroid hormone biosynthesis. The protein studied here was produced in Escherichia coli and doubly labeled with 13C and 15N. The diamagnetic 15N, 13C', 13C alpha, 13C beta, 1H alpha, and 1HN resonances from about 70% of the 124 amino acid residues for oxidized human ferredoxin and 80% of those for the reduced protein have been assigned primarily on the basis of results from three-dimensional, triple-resonance experiments. Secondary structure features for human ferredoxin in its oxidized and reduced states have been identified from a combination of chemical shift index and NOE data. Comparison of NMR results from the protein in its oxidized and reduced states indicates that structural changes accompany the change in the oxidation state of the [2Fe-2S] cluster. Major differences are localized at two regions: residues 29-31 and residues 109-124; the latter stretch forms the C-terminal region of the protein. The possible functional significance of these oxidation-state-dependent structural changes is discussed.

PMID: 9521718 [PubMed - indexed for MEDLINE]



Source: PubMed
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