1iu4
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(New page: 200px<br /><applet load="1iu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iu4, resolution 2.4Å" /> '''Crystal Structure Ana...)
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Revision as of 15:32, 20 November 2007
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Crystal Structure Analysis of the Microbial Transglutaminase
Overview
The crystal structure of a microbial transglutaminase from, Streptoverticillium mobaraense has been determined at 2.4 A resolution., The protein folds into a plate-like shape, and has one deep cleft at the, edge of the molecule. Its overall structure is completely different from, that of the factor XIII-like transglutaminase, which possesses a cysteine, protease-like catalytic triad. The catalytic residue, Cys(64), exists at, the bottom of the cleft. Asp(255) resides at the position nearest to, Cys(64) and is also adjacent to His(274). Interestingly, Cys(64), Asp(255), and His(274) superimpose well on the catalytic triad, "Cys-His-Asp" of the factor XIII-like transglutaminase, in this order. The, secondary structure frameworks around these residues are also similar to, each other. These results imply that both transglutaminases are related by, convergent evolution; however, the microbial transglutaminase has, developed a novel catalytic mechanism specialized for the cross-linking, reaction. The structure accounts well for the catalytic mechanism, in, which Asp(255) is considered to be enzymatically essential, as well as for, the causes of the higher reaction rate, the broader substrate specificity, and the lower deamidation activity of this enzyme.
About this Structure
1IU4 is a Single protein structure of sequence from Streptomyces mobaraensis. Active as Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 Full crystallographic information is available from OCA.
Reference
Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense., Kashiwagi T, Yokoyama K, Ishikawa K, Ono K, Ejima D, Matsui H, Suzuki E, J Biol Chem. 2002 Nov 15;277(46):44252-60. Epub 2002 Sep 7. PMID:12221081
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