3K1A
Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70Ile MoFe protein variant
Summary for 3K1A
| Entry DOI | 10.2210/pdb3k1a/pdb |
| Descriptor | Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (7 entities in total) |
| Functional Keywords | nitrogen fixation, mofe protein, nitrogenase, isoleucine, proton reduction, nitrogen, acetylene, hydride reduction, atp-binding, iron, iron-sulfur, metal-binding, nucleotide-binding, oxidoreductase, molybdenum |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 4 |
| Total formula weight | 232714.90 |
| Authors | Peters, J.W.,Sarma, R.,Barney, B.M.,Keable, S.,Seefeldt, L.C.,Dean, D.R. (deposition date: 2009-09-26, release date: 2010-02-16, Last modification date: 2023-09-06) |
| Primary citation | Sarma, R.,Barney, B.M.,Keable, S.,Dean, D.R.,Seefeldt, L.C.,Peters, J.W. Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70(Ile) MoFe protein variant J.Inorg.Biochem., 104:385-389, 2010 Cited by PubMed Abstract: The X-ray crystal structure is presented for a nitrogenase MoFe protein where the alpha subunit residue at position 70 (alpha-70(Val)) has been substituted by the amino acid isoleucine (alpha-70(Ile)). Substitution of alpha-70(Val) by alpha-70(Ile) results in a MoFe protein that is hampered in its ability to reduce a range of substrates including acetylene and N(2), yet retains normal proton reduction activity. The 2.3A structure of the alpha-70(Ile) MoFe protein is compared to the alpha-70(Val) wild-type MoFe protein, revealing that the delta methyl group of alpha-70(Val) is positioned over Fe6 within the active site FeMo-cofactor. This work provides strong crystallographic support for the previously proposed model that substrates bind and are reduced at a single 4Fe-4S face of the FeMo-cofactor and that when alpha-70(Val) is substituted by alpha-70(Ile) access of substrates to Fe6 of this face is effectively blocked. Furthermore the detailed examination of the structure provides the basis for understanding the ability to trap and characterize hydrides in the variant, contributing significantly to our understanding of substrate access and substrate reduction at the FeMo-cofactor active site of nitrogenase. PubMed: 20022118DOI: 10.1016/j.jinorgbio.2009.11.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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