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| <StructureSection load='1aw1' size='340' side='right'caption='[[1aw1]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1aw1' size='340' side='right'caption='[[1aw1]], [[Resolution|resolution]] 2.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1aw1]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"spirillum_marinum"_russell_1891 "spirillum marinum" russell 1891]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1aw1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Moritella_marina Moritella marina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AW1 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw1 OCA], [http://pdbe.org/1aw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aw1 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw1 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw1 OCA], [https://pdbe.org/1aw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw1 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw1 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/TPIS_MORMI TPIS_MORMI] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| ==See Also== | | ==See Also== |
- | *[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Spirillum marinum russell 1891]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Triose-phosphate isomerase]] | + | [[Category: Moritella marina]] |
- | [[Category: Maes, D]] | + | [[Category: Maes D]] |
- | [[Category: Wierenga, R K]] | + | [[Category: Wierenga RK]] |
- | [[Category: Zeelen, J P]] | + | [[Category: Zeelen JP]] |
- | [[Category: Isomerase]]
| + | |
- | [[Category: Psychrophilic]]
| + | |
- | [[Category: Vibrio marinus]]
| + | |
| Structural highlights
Function
TPIS_MORMI
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 purification and characterization of triose-phosphate isomerase from the psychrophilic bacterium Vibrio marinus (vTIM) is described. Crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex (at a 2.7-A resolution) are also presented. The optimal growth temperature of Vibrio marinus is 15 degrees C. Stability studies show that vTIM is an unstable protein with a half-life of only 10 min at 25 degrees C. The vTIM sequence is most closely related to the sequence of Escherichia coli TIM (eTIM) (66% identity), and several unique structural features described for eTIM are also seen in vTIM, but eTIM is considerably more stable. The Td values of vTIM and eTIM, determined by calorimetric studies, are 41 and 54 degrees C, respectively. Amino acid sequence comparison reveals that vTIM has an alanine in loop 8 (at position 238), whereas all other TIM sequences known to date have a serine. The vTIM mutant A238S was produced and characterized. Compared with wild type, the catalytic efficiency of the A238S mutant is somewhat reduced, and its stability is considerably increased.
Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.,Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D J Biol Chem. 1998 Jan 23;273(4):2199-206. PMID:9442062[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D. Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. J Biol Chem. 1998 Jan 23;273(4):2199-206. PMID:9442062
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