1lg5
From Proteopedia
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'''Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol''' | '''Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol''' | ||
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[[Category: Sauer-Eriksson, A E.]] | [[Category: Sauer-Eriksson, A E.]] | ||
[[Category: Sjoblom, B.]] | [[Category: Sjoblom, B.]] | ||
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Revision as of 20:53, 2 May 2008
Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol
Overview
Substitution of Pro for Thr199 in the active site of human carbonic anhydrase II (HCA II)(1) reduces its catalytic efficiency about 3000-fold. X-ray crystallographic structures of the T199P/C206S variant have been determined in complex with the substrate bicarbonate and with the inhibitors thiocyanate and beta-mercaptoethanol. The latter molecule is normally not an inhibitor of wild-type HCA II. All three ligands display novel binding interactions to the T199P/C206S mutant. The beta-mercaptoethanol molecule binds in the active site area with its sulfur atom tetrahedrally coordinated to the zinc ion. Thiocyanate binds tetrahedrally coordinated to the zinc ion in T199P/C206S, in contrast to its pentacoordinated binding to the zinc ion in wild-type HCA II. Bicarbonate binds to the mutant with two of its oxygens at the positions of the zinc water (Wat263) and Wat318 in wild-type HCA II. The environment of this area is more hydrophilic than the normal bicarbonate-binding site of HCA II situated in the hydrophobic part of the cavity normally occupied by the so-called deep water (Wat338). The observation of a new binding site for bicarbonate has implications for understanding the mechanism by which the main-chain amino group of Thr199 acquired an important role for orientation of the substrate during the evolution of the enzyme.
About this Structure
1LG5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant., Huang S, Sjoblom B, Sauer-Eriksson AE, Jonsson BH, Biochemistry. 2002 Jun 18;41(24):7628-35. PMID:12056894 Page seeded by OCA on Fri May 2 23:53:23 2008
