1hm5

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{{STRUCTURE_1hm5| PDB=1hm5 | SCENE= }}
{{STRUCTURE_1hm5| PDB=1hm5 | SCENE= }}
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'''CRYSTAL STRUCTURE ANALYSIS OF THE RABBIT D-GLUCOSE 6-PHOSPHATE ISOMERASE (NO LIGAND BOUND)'''
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===CRYSTAL STRUCTURE ANALYSIS OF THE RABBIT D-GLUCOSE 6-PHOSPHATE ISOMERASE (NO LIGAND BOUND)===
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==Overview==
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Phosphoglucose isomerase (PGI; EC 5.3.1.9) is the second enzyme in glycolysis, where it catalyzes the isomerization of D-glucose-6-phosphate to D-fructose-6-phosphate. It is the same protein as autocrine motility factor, differentiation and maturation mediator, and neuroleukin. Here, we report a new X-ray crystal structure of rabbit PGI (rPGI) without ligands bound in its active site. The structure was solved at 1.8A resolution by isomorphous phasing with a previously solved X-ray crystal structure of the rPGI dimer containing 6-phosphogluconate in its active site. Comparison of the new structure to previously reported structures enables identification of conformational changes that occur during binding of substrate or inhibitor molecules. Ligand binding causes an induced fit of regions containing amino acid residues 209-215, 245-259 and 385-389. This conformational change differs from the change previously reported to occur between the ring-opening and isomerization steps, in which the helix containing residues 513-521 moves toward the bound substrate. Differences between the liganded and unliganded structures are limited to the region within and close to the active-site pocket.
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(as it appears on PubMed at http://www.pubmed.gov), where 12368100 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12368100}}
==About this Structure==
==About this Structure==
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[[Category: Salmon, L.]]
[[Category: Salmon, L.]]
[[Category: Dimer]]
[[Category: Dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:00:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:23:26 2008''

Revision as of 05:23, 1 July 2008

Image:1hm5.png

Template:STRUCTURE 1hm5

CRYSTAL STRUCTURE ANALYSIS OF THE RABBIT D-GLUCOSE 6-PHOSPHATE ISOMERASE (NO LIGAND BOUND)

Template:ABSTRACT PUBMED 12368100

About this Structure

1HM5 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Conformational changes in phosphoglucose isomerase induced by ligand binding., Arsenieva D, Jeffery CJ, J Mol Biol. 2002 Oct 11;323(1):77-84. PMID:12368100

Page seeded by OCA on Tue Jul 1 08:23:26 2008

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