1h1l | pdb_00001h1l

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Revision as of 15:20, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1h1l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h1l, resolution 1.90Å" /> '''NITROGENASE MO-FE P...)
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NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT

File:1h1l.gif


1h1l, resolution 1.90Å

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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 MG, CL, CIT, CFM and CLF as [ligands]. Active as [[1]], with EC number [1.18.6.1]. 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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