1tzc | pdb_00001tzc

Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate

spinqualitylabelsall models 1tzc, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tzc is a 2 chain structure with sequence from Pyrae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, PA5, SO4 Related: 1tzb Gene: PAE1610 (PYRAE) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PGMI_PYRAE] Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglucose isomerase

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