1x9h
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1x9h.jpg|left|200px]] | + | [[Image:1x9h.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate''' | + | {{Structure |
| + | |PDB= 1x9h |SIZE=350|CAPTION= <scene name='initialview01'>1x9h</scene>, resolution 1.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= PAE1610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1X9H is a [ | + | 1X9H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9H OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes., Swan MK, Hansen T, Schonheit P, Davies C, Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:[http:// | + | Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes., Swan MK, Hansen T, Schonheit P, Davies C, Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15518558 15518558] |
[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 26: | Line 35: | ||
[[Category: pgi superfamily]] | [[Category: pgi superfamily]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:06:49 2008'' |
Revision as of 13:06, 20 March 2008
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | PAE1610 (Pyrobaculum aerophilum) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate
Overview
The crystal structure of a dual-specificity phosphoglucose/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has been determined in complex with glucose 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of mannose 6-phosphate (M6P) into the active site of the enzyme shows that the PMI activity of this enzyme may be due to the additional space imparted by a threonine. In PGIs from bacterial and eukaryotic sources, which cannot use M6P as a substrate, the equivalent residue is a glutamine. The increased space may permit rotation of the C2-C3 bond in M6P to facilitate abstraction of a proton from C2 by Glu203 and, after a further C2-C3 rotation of the resulting cis-enediolate, re-donation of a proton to C1 by the same residue. A proline residue (in place of a glycine in PGI) may also promote PMI activity by positioning the C1-O1 region of M6P. Thus, the PMI reaction in PaPGI/PMI probably uses a cis-enediol mechanism of catalysis, and this activity appears to arise from a subtle difference in the architecture of the enzyme, compared to bacterial and eukaryotic PGIs.
About this Structure
1X9H is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.
Reference
Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes., Swan MK, Hansen T, Schonheit P, Davies C, Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:15518558
Page seeded by OCA on Thu Mar 20 15:06:49 2008
