1mqf: Difference between revisions

Revision as of 00:59, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mqf.png

Template:STRUCTURE 1mqf

Compound I from Proteus mirabilis catalaseCompound I from Proteus mirabilis catalase

Template:ABSTRACT PUBMED 14646074

About this StructureAbout this Structure

1MQF is a Single protein structure of sequence from Proteus mirabilis. This structure supersedes the now removed PDB entry 2caf. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid., Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2163-8. Epub 2003, Nov 27. PMID:14646074

Page seeded by OCA on Thu Jul 3 00:59:05 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Compound I from Proteus mirabilis catalase'''
+===Compound I from Proteus mirabilis catalase===
-==Overview==
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-The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction.
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