1w0m
From Proteopedia
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| - | [[Image:1w0m.gif|left|200px]] | + | [[Image:1w0m.gif|left|200px]] |
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| - | '''TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX''' | + | {{Structure |
| + | |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> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W0M is a [ | + | 1W0M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0M OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15342242 15342242] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoproteus tenax]] | [[Category: Thermoproteus tenax]] | ||
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[[Category: triosephosphate isomerase]] | [[Category: triosephosphate isomerase]] | ||
| - | ''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 14:50:32 2008'' |
Revision as of 12:50, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||
| 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
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