1lgd

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{{STRUCTURE_1lgd| PDB=1lgd | SCENE= }}
{{STRUCTURE_1lgd| PDB=1lgd | SCENE= }}
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'''Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate'''
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===Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12056894}}
==About this Structure==
==About this Structure==
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[[Category: Sjoblom, B.]]
[[Category: Sjoblom, B.]]
[[Category: Hcaii mutant t199p-bct complex]]
[[Category: Hcaii mutant t199p-bct complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:53:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:52:28 2008''

Revision as of 17:52, 2 July 2008

Image:1lgd.png

Template:STRUCTURE 1lgd

Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate

Template:ABSTRACT PUBMED 12056894

About this Structure

1LGD 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

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