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2fkf

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[[Image:2fkf.gif|left|200px]]<br /><applet load="2fkf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fkf.gif|left|200px]]
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caption="2fkf, resolution 2.000&Aring;" />
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'''Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound'''<br />
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{{Structure
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|PDB= 2fkf |SIZE=350|CAPTION= <scene name='initialview01'>2fkf</scene>, resolution 2.000&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY=
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|GENE= algC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
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}}
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'''Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=G16:'>G16</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKF OCA].
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2FKF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKF OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16595672 16595672]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16595672 16595672]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: phosphoserine]]
[[Category: phosphoserine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:53:30 2008''

Revision as of 14:53, 20 March 2008


PDB ID 2fkf

Drag the structure with the mouse to rotate
, resolution 2.000Å
Ligands: and
Gene: algC (Pseudomonas aeruginosa)
Coordinates: save as pdb, mmCIF, xml



Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound


Overview

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.

About this Structure

2FKF 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

Page seeded by OCA on Thu Mar 20 16:53:30 2008

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