1y4i

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(New page: 200px<br /><applet load="1y4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4i, resolution 1.90&Aring;" /> '''Crystal structure of...)
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Revision as of 01:20, 25 November 2007

Image:1y4i.gif

1y4i, resolution 1.90Å

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Crystal structure of Citrobacter Freundii L-methionine-lyase

Overview

L-Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP) dependent, enzyme that catalyzes gamma-elimination of L-methionine. The crystal, structure of MGL from Citrobacter freundii has been determined at 1.9 A, resolution. The spatial fold of the protein is similar to those of MGLs, from Pseudomonas putida and Trichomonas vaginalis. The comparison of these, structures revealed that there are differences in PLP-binding residues and, positioning of the surrounding flexible loops.

About this Structure

1Y4I is a Single protein structure of sequence from Citrobacter freundii with SO4 as ligand. Active as Methionine gamma-lyase, with EC number 4.4.1.11 Full crystallographic information is available from OCA.

Reference

Structure of Citrobacter freundii L-methionine gamma-lyase., Mamaeva DV, Morozova EA, Nikulin AD, Revtovich SV, Nikonov SV, Garber MB, Demidkina TV, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt, 6):546-9. Epub 2005 Jun 1. PMID:16511092

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