2fkm
From Proteopedia
(New page: 200px<br /><applet load="2fkm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fkm, resolution 1.900Å" /> '''PMM/PGM S108D mutan...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2fkm.gif|left|200px]]<br /><applet load="2fkm" size=" | + | [[Image:2fkm.gif|left|200px]]<br /><applet load="2fkm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fkm, resolution 1.900Å" /> | caption="2fkm, resolution 1.900Å" /> | ||
'''PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound'''<br /> | '''PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from | + | 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== | ==About this Structure== | ||
| - | 2FKM 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 G16 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2FKM 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]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKM OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beamer, L | + | [[Category: Beamer, L J.]] |
| - | [[Category: Regni, C | + | [[Category: Regni, C A.]] |
[[Category: G16]] | [[Category: G16]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| Line 22: | Line 22: | ||
[[Category: enzyme-metal complex]] | [[Category: enzyme-metal complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:21 2008'' |
Revision as of 15:22, 21 February 2008
|
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 with and as ligands. Active as Phosphomannomutase, with EC number 5.4.2.8 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 Feb 21 17:22:21 2008
