1H1L
NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT
Summary for 1H1L
Entry DOI | 10.2210/pdb1h1l/pdb |
Related | 1QGU 1QH1 1QH8 |
Descriptor | NITROGENASE MOLYBDENUM IRON PROTEIN ALPHA CHAIN, NITROGENASE MOLYBDENUM IRON PROTEIN BETA CHAIN, CITRIC ACID, ... (8 entities in total) |
Functional Keywords | biological nitrogen fixation, nitrogen metabolism, molybdoenzymes, electron transfer, oxidoreductase |
Biological source | KLEBSIELLA PNEUMONIAE More |
Total number of polymer chains | 4 |
Total formula weight | 227960.82 |
Authors | Mayer, S.M.,Gormal, C.A.,Smith, B.E.,Lawson, D.M. (deposition date: 2002-07-18, release date: 2002-07-29, Last modification date: 2023-12-13) |
Primary citation | Mayer, S.M.,Gormal, C.A.,Smith, B.E.,Lawson, D.M. Crystallographic Analysis of the Mofe Protein of Nitrogenase from a Nifv Mutant of Klebsiella Pneumoniae Identifies Citrate as a Ligand to the Molybdenum of Iron Molybdenum Cofactor (Femoco). J.Biol.Chem., 277:35263-, 2002 Cited by PubMed Abstract: The x-ray crystal structure of NifV(-) Klebsiella pneumoniae nitrogenase MoFe protein (NifV(-) Kp1) has been determined and refined to a resolution of 1.9 A. This is the first structure for a nitrogenase MoFe protein with an altered cofactor. Moreover, it is the first direct evidence that the organic acid citrate is not just present, but replaces homocitrate as a ligand to the molybdenum atom of the iron molybdenum cofactor (FeMoco). Subsequent refinement of the structure revealed that the citrate was present at reduced occupancy. PubMed: 12133839DOI: 10.1074/JBC.M205888200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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