This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1tzb
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1tzb.gif|left|200px]] | + | [[Image:1tzb.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of native phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum''' | + | {{Structure |
| + | |PDB= 1tzb |SIZE=350|CAPTION= <scene name='initialview01'>1tzb</scene>, resolution 1.16Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=178306 Pyrobaculum aerophilum str. IM2]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of native phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1TZB is a [ | + | 1TZB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._im2 Pyrobaculum aerophilum str. im2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZB OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15252053 15252053] |
[[Category: Pyrobaculum aerophilum str. im2]] | [[Category: Pyrobaculum aerophilum str. im2]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 24: | Line 33: | ||
[[Category: pgi family]] | [[Category: pgi family]] | ||
| - | ''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 14:25:11 2008'' |
Revision as of 12:25, 20 March 2008
| |||||||
| , resolution 1.16Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | PAE1610 (Pyrobaculum aerophilum str. IM2) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 14:25:11 2008
