2fkm

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{{STRUCTURE_2fkm| PDB=2fkm | SCENE= }}
{{STRUCTURE_2fkm| PDB=2fkm | SCENE= }}
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'''PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound'''
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===PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound===
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==Overview==
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The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars. The reaction entails two phosphoryl transfers, with an intervening 180 degrees reorientation of the reaction intermediate (e.g. glucose 1,6-bisphosphate) during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is, thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Structural characterization of two PMM/PGM-intermediate complexes with glucose 1,6-bisphosphate provides new insights into the reaction catalyzed by the enzyme, including the reorientation of the intermediate. Kinetic analyses of site-directed mutants prompted by the structural studies reveal active site residues critical for maintaining association with glucose 1,6-bisphosphate during its unique dynamic reorientation in the active site of PMM/PGM.
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The line below this paragraph, {{ABSTRACT_PUBMED_16595672}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16595672 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16595672}}
==About this Structure==
==About this Structure==
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[[Category: Enzyme-ligand complex]]
[[Category: Enzyme-ligand complex]]
[[Category: Enzyme-metal complex]]
[[Category: Enzyme-metal complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:00:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:12:12 2008''

Revision as of 15:12, 27 July 2008

Template:STRUCTURE 2fkm

PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound

Template:ABSTRACT PUBMED 16595672

About this Structure

2FKM is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme., Regni C, Schramm AM, Beamer LJ, J Biol Chem. 2006 Jun 2;281(22):15564-71. Epub 2006 Apr 4. PMID:16595672

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