1g0d
From Proteopedia
(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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| - | [[Image:1g0d.gif|left|200px]]<br /><applet load="1g0d" size=" | + | [[Image:1g0d.gif|left|200px]]<br /><applet load="1g0d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g0d, resolution 2.5Å" /> | caption="1g0d, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF RED SEA BREAM TRANSGLUTAMINASE'''<br /> | '''CRYSTAL STRUCTURE OF RED SEA BREAM TRANSGLUTAMINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the tissue-type transglutaminase from red sea | + | 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== | ==About this Structure== | ||
| - | 1G0D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pagrus_major Pagrus major] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1G0D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pagrus_major Pagrus major] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1G0D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tissue transglutaminase]] | [[Category: tissue transglutaminase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:35 2008'' |
Revision as of 10:44, 21 February 2008
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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 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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