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1w0m

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{{STRUCTURE_1w0m| PDB=1w0m | SCENE= }}
{{STRUCTURE_1w0m| PDB=1w0m | SCENE= }}
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'''TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX'''
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===TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15342242}}
==About this Structure==
==About this Structure==
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[[Category: Glycolysis]]
[[Category: Glycolysis]]
[[Category: Triosephosphate isomerase]]
[[Category: Triosephosphate isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:35:40 2008''

Revision as of 04:35, 28 July 2008

Image:1w0m.png

Template:STRUCTURE 1w0m

TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX

Template:ABSTRACT PUBMED 15342242

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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