1ggt: Difference between revisions
New page: left|200px<br /> <applet load="1ggt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggt, resolution 2.65Å" /> '''THREE-DIMENSIONAL S... |
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[[Image:1ggt.gif|left|200px]]<br /> | [[Image:1ggt.gif|left|200px]]<br /><applet load="1ggt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1ggt, resolution 2.65Å" /> | caption="1ggt, resolution 2.65Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''<br /> | ||
==Overview== | ==Overview== | ||
Mechanical stability in many biological materials is provided by the | Mechanical stability in many biological materials is provided by the crosslinking of large structural proteins with gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure of human recombinant factor XIII (EC 2.3.2.13 zymogen; protein-glutamine:amine gamma-glutamyltransferase a chain), a transglutaminase zymogen, has been solved at 2.8-A resolution by x-ray crystallography. This structure shows that each chain of the homodimeric protein is folded into four sequential domains. A catalytic triad reminiscent of that observed in cysteine proteases has been identified in the core domain. The amino-terminal activation peptide of each subunit crosses the dimer interface and partially occludes the opening of the catalytic cavity in the second subunit, preventing substrate binding to the zymogen. A proposal for the mechanism of activation by thrombin and calcium is made that details the structural events leading to active factor XIIIa'. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1GGT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] Full crystallographic information is available from [http:// | 1GGT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein-glutamine gamma-glutamyltransferase]] | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bishop, P | [[Category: Bishop, P D.]] | ||
[[Category: Pedersen, L | [[Category: Pedersen, L C.]] | ||
[[Category: Stenkamp, R | [[Category: Stenkamp, R E.]] | ||
[[Category: Teller, D | [[Category: Teller, D C.]] | ||
[[Category: Trong, I | [[Category: Trong, I L.]] | ||
[[Category: Yee, V | [[Category: Yee, V C.]] | ||
[[Category: blood coagulation]] | [[Category: blood coagulation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:54 2008'' | ||
Revision as of 10:49, 21 February 2008
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THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII
Overview
Mechanical stability in many biological materials is provided by the crosslinking of large structural proteins with gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure of human recombinant factor XIII (EC 2.3.2.13 zymogen; protein-glutamine:amine gamma-glutamyltransferase a chain), a transglutaminase zymogen, has been solved at 2.8-A resolution by x-ray crystallography. This structure shows that each chain of the homodimeric protein is folded into four sequential domains. A catalytic triad reminiscent of that observed in cysteine proteases has been identified in the core domain. The amino-terminal activation peptide of each subunit crosses the dimer interface and partially occludes the opening of the catalytic cavity in the second subunit, preventing substrate binding to the zymogen. A proposal for the mechanism of activation by thrombin and calcium is made that details the structural events leading to active factor XIIIa'.
Disease
Known disease associated with this structure: Factor XIIIA deficiency OMIM:[134570]
About this Structure
1GGT is a Single protein structure of sequence from Homo sapiens. Active as Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII., Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC, Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. PMID:7913750
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