1u0f: Difference between revisions

Revision as of 12:05, 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:1u0f.png

Template:STRUCTURE 1u0f

Crystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphateCrystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphate

Template:ABSTRACT PUBMED 15342241

About this StructureAbout this Structure

1U0F is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of mouse phosphoglucose isomerase at 1.6A resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening., Graham Solomons JT, Zimmerly EM, Burns S, Krishnamurthy N, Swan MK, Krings S, Muirhead H, Chirgwin J, Davies C, J Mol Biol. 2004 Sep 17;342(3):847-60. PMID:15342241

Page seeded by OCA on Tue Jul 29 12:05:43 2008

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

OCA

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-[[Image:1u0f.jpg|left|200px]]
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 {{STRUCTURE_1u0f|  PDB=1u0f  |  SCENE=  }}
-'''Crystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphate'''
+===Crystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphate===
-==Overview==
+<!--
-Phosphoglucose isomerase (PGI) is an enzyme of glycolysis that interconverts glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) but, outside the cell, is a multifunctional cytokine. High-resolution crystal structures of the enzyme from mouse have been determined in native form and in complex with the inhibitor erythrose 4-phosphate, and with the substrate glucose 6-phosphate. In the substrate-bound structure, the glucose sugar is observed in both straight-chain and ring forms. This structure supports a specific role for Lys518 in enzyme-catalyzed ring opening and we present a "push-pull" mechanism in which His388 breaks the O5-C1 bond by donating a proton to the ring oxygen atom and, simultaneously, Lys518 abstracts a proton from the C1 hydroxyl group. The reverse occurs in ring closure. The transition from ring form to straight-chain substrate is achieved through rotation of the C3-C4 bond, which brings the C1-C2 region into close proximity to Glu357, the base catalyst for the isomerization step. The structure with G6P also explains the specificity of PGI for glucose 6-phosphate over mannose 6-isomerase (M6P). To isomerize M6P to F6P requires a rotation of its C2-C3 bond but in PGI this is sterically blocked by Gln511.
+The line below this paragraph, {{ABSTRACT_PUBMED_15342241}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15342241 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15342241}}
 ==About this Structure==
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 [[Category: Aldose-ketose isomerase]]
 [[Category: Dimer]]
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