2bi7: Difference between revisions

Revision as of 11:31, 29 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:2bi7.png

Template:STRUCTURE 2bi7

UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE OXIDISED FADUDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE OXIDISED FAD

Template:ABSTRACT PUBMED 15843027

About this StructureAbout this Structure

2BI7 is a Single protein structure of sequence from Klebsiella pneumoniae. This structure supersedes the now removed PDB entry 1usj. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:15843027

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OCA

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-'''UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE OXIDISED FAD'''
+===UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE OXIDISED FAD===
-==Overview==
+<!--
-Uridine diphosphogalactofuranose (UDP-Galf) is the precursor of the d-galactofuranose sugar found in bacterial and parasitic cell walls, including those of many pathogens. UDP-Galf is made from UDP-galactopyranose by the enzyme UDP-galactopyranose mutase. The enzyme requires the reduced FADH- co-factor for activity. The structure of the Mycobacterium tuberculosis mutase with FAD has been determined to 2.25 A. The structures of Klebsiella pneumoniae mutase with FAD and with FADH- bound have been determined to 2.2 A and 2.35 A resolution, respectively. This is the first report of the FADH(-)-containing structure. Two flavin-dependent mechanisms for the enzyme have been proposed, one, which involves a covalent adduct being formed at the flavin and the other based on electron transfer. Using our structural data, we have examined the two mechanisms. The electron transfer mechanism is consistent with the structural data, not surprisingly, since it makes fewer demands on the precise positioning of atoms. A model based on a covalent adduct FAD requires repositioning of the enzyme active site and would appear to require the isoalloxazine ring of FADH- to buckle in a particular way. However, the FADH- structure reveals that the isoalloxazine ring buckles in the opposite sense, this apparently requires the covalent adduct to trigger profound conformational changes in the protein or to buckle the FADH- opposite to that seen in the apo structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_15843027}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15843027}}
 ==About this Structure==
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 [[Category: Isomerase]]
 [[Category: Lipopolysaccharide biosynthesis]]
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