1h1l

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{{STRUCTURE_1h1l| PDB=1h1l | SCENE= }}
{{STRUCTURE_1h1l| PDB=1h1l | SCENE= }}
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'''NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT'''
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===NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12133839 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12133839}}
==About this Structure==
==About this Structure==
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[[Category: Nitrogen metabolism]]
[[Category: Nitrogen metabolism]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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Revision as of 03:28, 1 July 2008

Image:1h1l.png

Template:STRUCTURE 1h1l

NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT

Template:ABSTRACT PUBMED 12133839

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

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