1h1l
From Proteopedia
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, resolution 1.90Å | |||||||
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Sites: | |||||||
Ligands: | , , , and | ||||||
Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT
Overview
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.
About this Structure
1H1L is a Protein complex structure of sequences from Klebsiella pneumoniae. Full crystallographic information is available from OCA.
Reference
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)., Mayer SM, Gormal CA, Smith BE, Lawson DM, J Biol Chem. 2002 Sep 20;277(38):35263-6. Epub 2002 Jul 19. PMID:12133839
Page seeded by OCA on Thu Mar 20 11:30:54 2008