ISDA: 1G5P

Deposition Date 2000-11-01

Release Date 2001-01-31

Last Version Date 2026-08-12

Entry Detail

PDB ID:

1G5P

Keywords:

OXIDOREDUCTASE

Title:

NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII

Biological Source:

Source Organism(s):

Azotobacter vinelandii (Taxon ID: 354)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.20 Å

R-Value Free:

0.29

R-Value Work:

0.22

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:NITROGENASE IRON PROTEIN
Gene (Uniprot):nifH1
Chain IDs:A, B
Chain Length:289
Number of Molecules:2
Biological Source:Azotobacter vinelandii

UniProt ID:P00459 Pfam ID:PF00142 EC:1.18.6.1

Ligand Molecules

SF4

Primary Citation

Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii.

Strop, P, Takahara, P.M, Chiu, H, Angove, H.C, Burgess, B.K, Rees, D.C.Show

Biochemistry 40 651 656 (2001)

PMID: 11170381 DOI: 10.1021/bi0016467

Abstact

The structure of the nitrogenase iron protein from Azotobacter vinelandii in the all-ferrous [4Fe-4S](0) form has been determined to 2.25 A resolution by using the multiwavelength anomalous diffraction (MAD) phasing technique. The structure demonstrates that major conformational changes are not necessary either in the iron protein or in the cluster to accommodate cluster reduction to the [4Fe-4S](0) oxidation state. A survey of [4Fe-4S] clusters coordinated by four cysteine ligands in proteins of known structure reveals that the [4Fe-4S] cluster of the iron protein has the largest accessible surface area, suggesting that solvent exposure may be relevant to the ability of the iron protein to exist in three oxidation states.

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Primary Citation of related structures

Abstact

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