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1x0l

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{{STRUCTURE_1x0l| PDB=1x0l | SCENE= }}
{{STRUCTURE_1x0l| PDB=1x0l | SCENE= }}
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'''Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus'''
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===Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus===
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==Overview==
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The crystal structure of homoisocitrate dehydrogenase involved in lysine biosynthesis from Thermus thermophilus (TtHICDH) was determined at 1.85-A resolution. Arg85, which was shown to be a determinant for substrate specificity in our previous study, is positioned close to the putative substrate binding site and interacts with Glu122. Glu122 is highly conserved in the equivalent position in the primary sequence of ICDH and archaeal 3-isopropylmalate dehydrogenase (IPMDH) but interacts with main- and side-chain atoms in the same domain in those paralogs. In addition, a conserved Tyr residue (Tyr125 in TtHICDH) which extends its side chain toward a substrate and thus has a catalytic function in the related beta-decarboxylating dehydrogenases, is flipped out of the substrate-binding site. These results suggest the possibility that the conformation of the region containing Glu122-Tyr125 is changed upon substrate binding in TtHICDH. The crystal structure of TtHICDH also reveals that the arm region is involved in tetramer formation via hydrophobic interactions and might be responsible for the high thermotolerance. Mutation of Val135, located in the dimer-dimer interface and involved in the hydrophobic interaction, to Met alters the enzyme to a dimer (probably due to steric perturbation) and markedly decreases the thermal inactivation temperature. Both the crystal structure and the mutation analysis indicate that tetramer formation is involved in the extremely high thermotolerance of TtHICDH.
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(as it appears on PubMed at http://www.pubmed.gov), where 16166541 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16166541}}
==About this Structure==
==About this Structure==
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[[Category: Lysine biosynthesis]]
[[Category: Lysine biosynthesis]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:22:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:17:24 2008''

Revision as of 13:17, 28 July 2008

Image:1x0l.png

Template:STRUCTURE 1x0l

Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus

Template:ABSTRACT PUBMED 16166541

About this Structure

1X0L is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance., Miyazaki J, Asada K, Fushinobu S, Kuzuyama T, Nishiyama M, J Bacteriol. 2005 Oct;187(19):6779-88. PMID:16166541

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