1g0d: Difference between revisions

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<StructureSection load='1g0d' size='340' side='right'caption='[[1g0d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1g0d' size='340' side='right'caption='[[1g0d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g0d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1g0d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pagrus_major Pagrus major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0d OCA], [https://pdbe.org/1g0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0d RCSB], [https://www.ebi.ac.uk/pdbsum/1g0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0d ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0d OCA], [https://pdbe.org/1g0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0d RCSB], [https://www.ebi.ac.uk/pdbsum/1g0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TGM2_PAGMA TGM2_PAGMA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g0d ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g0d ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11080504</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1g0d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
[[Category: Pagrus major]]
[[Category: Ishikawa, K]]
[[Category: Ishikawa K]]
[[Category: Nio, N]]
[[Category: Nio N]]
[[Category: Noguchi, K]]
[[Category: Noguchi K]]
[[Category: Ohtsuka, T]]
[[Category: Ohtsuka T]]
[[Category: Suzuki, E]]
[[Category: Suzuki E]]
[[Category: Yokoyama, K]]
[[Category: Yokoyama K]]
[[Category: Acyltransferase]]
[[Category: Tissue transglutaminase]]
[[Category: Transferase]]

Latest revision as of 16:23, 13 March 2024

CRYSTAL STRUCTURE OF RED SEA BREAM TRANSGLUTAMINASECRYSTAL STRUCTURE OF RED SEA BREAM TRANSGLUTAMINASE

Structural highlights

1g0d is a 1 chain structure with sequence from Pagrus major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TGM2_PAGMA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1g0d, resolution 2.50Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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