1G1M

ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII

Summary for 1G1M

• Entry DOI: 10.2210/pdb1g1m/pdb
• Related: 1CP2 1N2C 3NIP
• Descriptor: NITROGENASE IRON PROTEIN, IRON/SULFUR CLUSTER (3 entities in total)
• Functional Keywords: iron protein, oxidoreductase, nitrogenase, all-ferrous
• Biological source: Azotobacter vinelandii
• Total number of polymer chains: 2
• Total formula weight: 63185.73

Authors

Strop, P.,Takahara, P.M.,Chiu, H.-J.,Angove, H.C.,Burgess, B.K.,Rees, D.C. (deposition date: 2000-10-12, release date: 2001-01-31, Last modification date: 2024-02-07)

Primary citation

Strop, P.,Takahara, P.M.,Chiu, H.,Angove, H.C.,Burgess, B.K.,Rees, D.C.
Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii.
Biochemistry, 40:651-656, 2001

PubMed Abstract: 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.

PubMed: 11170381
DOI: 10.1021/bi0016467

Experimental method

X-RAY DIFFRACTION (2.25 Å)