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1H1L

NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT

Summary for 1H1L
Entry DOI10.2210/pdb1h1l/pdb
Related1QGU 1QH1 1QH8
DescriptorNITROGENASE MOLYBDENUM IRON PROTEIN ALPHA CHAIN, NITROGENASE MOLYBDENUM IRON PROTEIN BETA CHAIN, CITRIC ACID, ... (8 entities in total)
Functional Keywordsbiological nitrogen fixation, nitrogen metabolism, molybdoenzymes, electron transfer, oxidoreductase
Biological sourceKLEBSIELLA PNEUMONIAE
More
Total number of polymer chains4
Total formula weight227960.82
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 citationMayer, 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: 12133839
DOI: 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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数据于2025-08-27公开中

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