1w0m
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1w0m |SIZE=350|CAPTION= <scene name='initialview01'>1w0m</scene>, resolution 2.5Å | |PDB= 1w0m |SIZE=350|CAPTION= <scene name='initialview01'>1w0m</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+H'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+H'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0m OCA], [http://www.ebi.ac.uk/pdbsum/1w0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w0m RCSB]</span> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: Tjaden, B.]] | [[Category: Tjaden, B.]] | ||
[[Category: Walden, H.]] | [[Category: Walden, H.]] | ||
| - | [[Category: PO4]] | ||
[[Category: gluconeogenesis]] | [[Category: gluconeogenesis]] | ||
[[Category: glycolysis]] | [[Category: glycolysis]] | ||
[[Category: triosephosphate isomerase]] | [[Category: triosephosphate isomerase]] | ||
| - | ''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 00:29:30 2008'' |
Revision as of 21:29, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX
Overview
Triosephophate isomerase (TIM) is a dimeric enzyme in eucarya, bacteria and mesophilic archaea. In hyperthermophilic archaea, however, TIM exists as a tetramer composed of monomers that are about 10% shorter than other eucaryal and bacterial TIM monomers. We report here the crystal structure of TIM from Thermoproteus tenax, a hyperthermophilic archaeon that has an optimum growth temperature of 86 degrees C. The structure was determined from both a hexagonal and an orthorhombic crystal form to resolutions of 2.5A and 2.3A, and refined to R-factors of 19.7% and 21.5%, respectively. In both crystal forms, T.tenax TIM exists as a tetramer of the familiar (betaalpha)(8)-barrel. In solution, however, and unlike other hyperthermophilic TIMs, the T.tenax enzyme exhibits an equilibrium between inactive dimers and active tetramers, which is shifted to the tetramer state through a specific interaction with glycerol-1-phosphate dehydrogenase of T.tenax. This observation is interpreted in physiological terms as a need to reduce the build-up of thermolabile metabolic intermediates that would be susceptible to destruction by heat. A detailed structural comparison with TIMs from organisms with growth optima ranging from 15 degrees C to 100 degrees C emphasizes the importance in hyperthermophilic proteins of the specific location of ionic interactions for thermal stability rather than their numbers, and shows a clear correlation between the reduction of heat-labile, surface-exposed Asn and Gln residues with thermoadaptation. The comparison confirms the increase in charged surface-exposed residues at the expense of polar residues.
About this Structure
1W0M is a Single protein structure of sequence from Thermoproteus tenax. Full crystallographic information is available from OCA.
Reference
Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature., Walden H, Taylor GL, Lorentzen E, Pohl E, Lilie H, Schramm A, Knura T, Stubbe K, Tjaden B, Hensel R, J Mol Biol. 2004 Sep 17;342(3):861-75. PMID:15342242
Page seeded by OCA on Mon Mar 31 00:29:30 2008
