1g0d
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(New page: 200px<br /><applet load="1g0d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g0d, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:27, 20 November 2007
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CRYSTAL STRUCTURE OF RED SEA BREAM TRANSGLUTAMINASE
Overview
The crystal structure of the tissue-type transglutaminase from red sea, bream liver (fish-derived transglutaminase, FTG) has been determined at, 2.5-A resolution using the molecular replacement method, based on the, crystal structure of human blood coagulation factor XIII, which is a, transglutaminase zymogen. The model contains 666 residues of a total of, 695 residues, 382 water molecules, and 1 sulfate ion. FTG consists of four, domains, and its overall and active site structures are similar to those, of human factor XIII. However, significant structural differences are, observed in both the acyl donor and acyl acceptor binding sites, which, account for the difference in substrate preferences. The active site of, the enzyme is inaccessible to the solvent, because the catalytic Cys-272, hydrogen-bonds to Tyr-515, which is thought to be displaced upon acyl, donor binding to FTG. It is postulated that the binding of an, inappropriate substrate to FTG would lead to inactivation of the enzyme, because of the formation of a new disulfide bridge between Cys-272 and the, adjacent Cys-333 immediately after the displacement of Tyr-515., Considering the mutational studies previously reported on the tissue-type, transglutaminases, we propose that Cys-333 and Tyr-515 are important in, strictly controlling the enzymatic activity of FTG.
About this Structure
1G0D is a Single protein structure of sequence from Pagrus major with SO4 as ligand. Active as Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 Full crystallographic information is available from OCA.
Reference
Crystal structure of red sea bream transglutaminase., Noguchi K, Ishikawa K, Yokoyama Ki, Ohtsuka T, Nio N, Suzuki E, J Biol Chem. 2001 Apr 13;276(15):12055-9. Epub 2000 Nov 15. PMID:11080504
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