1h1l

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Image:1h1l.jpg

1h1l, resolution 1.90Å

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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 with , , , and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Known structural/functional Site: . 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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