1tzc
From Proteopedia
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'''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate''' | '''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate''' | ||
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[[Category: Schoenheit, P.]] | [[Category: Schoenheit, P.]] | ||
[[Category: Swan, M K.]] | [[Category: Swan, M K.]] | ||
| - | [[Category: | + | [[Category: Crenarchaeon]] |
| - | [[Category: | + | [[Category: Enzyme]] |
| - | [[Category: | + | [[Category: Hyperthermophile]] |
| - | [[Category: | + | [[Category: Pgi family]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:33:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:33, 3 May 2008
Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate
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
1TZC 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 Page seeded by OCA on Sat May 3 10:33:12 2008
