2nip
From Proteopedia
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NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII
Overview
The nitrogenase iron (Fe) protein performs multiple functions during, biological nitrogen fixation, including mediating the mechanistically, essential coupling between ATP hydrolysis and electron transfer to the, nitrogenase molybdenum iron (MoFe) protein during substrate reduction, and, participating in the biosynthesis and insertion of the FeMo-cofactor into, the MoFe-protein. To establish a structural framework for addressing the, diverse functions of Fe-protein, crystal structures of the Fe-proteins, from Azotobacter vinelandii and Clostridium pasteurianum have been, determined at resolutions of 2.2 A and 1.93 A, respectively. These two, Fe-proteins are among the more diverse in terms of amino acid sequence and, biochemical properties. As described initially for the A. vinelandii, ... [(full description)]
About this Structure
2NIP is a [Single protein] structure of sequence from [Azotobacter vinelandii] with SF4 as [ligand]. Active as [[1]], with EC number [1.18.6.1]. Full crystallographic information is available from [OCA].
Reference
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum., Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC, J Mol Biol. 1998 Jul 24;280(4):669-85. PMID:9677296
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