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1tzb
From Proteopedia
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|PDB= 1tzb |SIZE=350|CAPTION= <scene name='initialview01'>1tzb</scene>, resolution 1.16Å | |PDB= 1tzb |SIZE=350|CAPTION= <scene name='initialview01'>1tzb</scene>, resolution 1.16Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PAE1610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 Pyrobaculum aerophilum str. IM2]) | |GENE= PAE1610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 Pyrobaculum aerophilum str. IM2]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tzc|1TZC]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzb OCA], [http://www.ebi.ac.uk/pdbsum/1tzb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tzb RCSB]</span> | ||
}} | }} | ||
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[[Category: Schoenheit, P.]] | [[Category: Schoenheit, P.]] | ||
[[Category: Swan, M K.]] | [[Category: Swan, M K.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: crenarchaeon]] | [[Category: crenarchaeon]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
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[[Category: pgi family]] | [[Category: pgi family]] | ||
| - | ''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 00:03:09 2008'' |
Revision as of 21:03, 30 March 2008
| |||||||
| , resolution 1.16Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PAE1610 (Pyrobaculum aerophilum str. IM2) | ||||||
| Related: | 1TZC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of native phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum
Overview
The crystal structure of a dual specificity phosphoglucose isomerase (PGI)/phosphomannose isomerase from Pyrobaculum aerophilum (PaPGI/PMI) has been determined in native form at 1.16-A resolution and in complex with the enzyme inhibitor 5-phosphoarabinonate at 1.45-A resolution. The similarity of its fold, with the inner core structure of PGIs from eubacterial and eukaryotic sources, confirms this enzyme as a member of the PGI superfamily. The almost total conservation of amino acids in the active site, including the glutamate base catalyst, shows that PaPGI/PMI uses the same catalytic mechanisms for both ring opening and isomerization for the interconversion of glucose 6-phosphate (Glc-6-P) to fructose 6-phosphate (Fru-6-P). The lack of structural differences between native and inhibitor-bound enzymes suggests this activity occurs without any of the conformational changes that are the hallmark of the well characterized PGI family. The lack of a suitable second base in the active site of PaPGI/PMI argues against a PMI mechanism involving a trans-enediol intermediate. Instead, PMI activity may be the result of additional space in the active site imparted by a threonine, in place of a glutamine in other PGI enzymes, which could permit rotation of the C-2-C-3 bond of mannose 6-phosphate.
About this Structure
1TZB is a Single protein structure of sequence from Pyrobaculum aerophilum str. im2. Full crystallographic information is available from OCA.
Reference
A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution., Swan MK, Hansen T, Schonheit P, Davies C, J Biol Chem. 2004 Sep 17;279(38):39838-45. Epub 2004 Jul 13. PMID:15252053
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