2zc0: Difference between revisions

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<StructureSection load='2zc0' size='340' side='right'caption='[[2zc0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2zc0' size='340' side='right'caption='[[2zc0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2zc0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'caldococcus_litoralis'_z-1301 'caldococcus litoralis' z-1301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZC0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZC0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2zc0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZC0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.3&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine--glyoxylate_transaminase Alanine--glyoxylate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zc0 OCA], [http://pdbe.org/2zc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zc0 RCSB], [http://www.ebi.ac.uk/pdbsum/2zc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zc0 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=2zc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zc0 OCA], [https://pdbe.org/2zc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zc0 RCSB], [https://www.ebi.ac.uk/pdbsum/2zc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zc0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9C4M4_THELI Q9C4M4_THELI]
== 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=2zc0 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=2zc0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a novel alanine:glyoxylate aminotransferase from the hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A resolution. The asymmetric unit contains four homologous subunits and the functional tetramer is generated by noncrystallographic 222 symmetry. Although the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme showed a high degree of similarity to those of aspartate aminotransferase from Thermus thermophilus HB8, the amino-acid residues involved in substrate binding in the aspartate aminotransferase are only partially conserved in the Thermococcus litoralis enzyme. This may account for the difference in the substrate specificities of the two enzymes.
Structure of an archaeal alanine:glyoxylate aminotransferase.,Sakuraba H, Yoneda K, Takeuchi K, Tsuge H, Katunuma N, Ohshima T Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):696-9. Epub 2008 May 14. PMID:18560158<ref>PMID:18560158</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zc0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caldococcus litoralis z-1301]]
[[Category: Alanine--glyoxylate transaminase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ohshima, T]]
[[Category: Thermococcus litoralis]]
[[Category: Sakuraba, H]]
[[Category: Ohshima T]]
[[Category: Tsuge, H]]
[[Category: Sakuraba H]]
[[Category: Yoneda, K]]
[[Category: Tsuge H]]
[[Category: Alanine:glyoxylate aminotransferase]]
[[Category: Yoneda K]]
[[Category: Archaea]]
[[Category: Thermococcus litorali]]
[[Category: Transferase]]
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