2fkm
From Proteopedia
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|PDB= 2fkm |SIZE=350|CAPTION= <scene name='initialview01'>2fkm</scene>, resolution 1.900Å | |PDB= 2fkm |SIZE=350|CAPTION= <scene name='initialview01'>2fkm</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene> | + | |LIGAND= <scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] </span> |
|GENE= AlgC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | |GENE= AlgC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k35|1K35]], [[1k2y|1K2Y]], [[1pcj|1PCJ]], [[1pcm|1PCM]], [[1p5d|1P5D]], [[1p5g|1P5G]], [[2fkf|2FKF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkm OCA], [http://www.ebi.ac.uk/pdbsum/2fkm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fkm RCSB]</span> | ||
}} | }} | ||
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[[Category: Beamer, L J.]] | [[Category: Beamer, L J.]] | ||
[[Category: Regni, C A.]] | [[Category: Regni, C A.]] | ||
| - | [[Category: G16]] | ||
| - | [[Category: ZN]] | ||
[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
[[Category: enzyme-ligand complex]] | [[Category: enzyme-ligand complex]] | ||
[[Category: enzyme-metal complex]] | [[Category: enzyme-metal complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:04:08 2008'' |
Revision as of 00:04, 31 March 2008
| |||||||
| , resolution 1.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | AlgC (Pseudomonas aeruginosa) | ||||||
| Activity: | Phosphomannomutase, with EC number 5.4.2.8 | ||||||
| Related: | 1K35, 1K2Y, 1PCJ, 1PCM, 1P5D, 1P5G, 2FKF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PMM/PGM S108D mutant 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
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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