2ze3: Difference between revisions

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<StructureSection load='2ze3' size='340' side='right'caption='[[2ze3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='2ze3' size='340' side='right'caption='[[2ze3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ze3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ccug_51391 Ccug 51391]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZE3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZE3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ze3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_ficus Deinococcus ficus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZE3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</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]] 1.65&#8491;</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=2ze3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ze3 OCA], [http://pdbe.org/2ze3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ze3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ze3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ze3 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</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=2ze3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ze3 OCA], [https://pdbe.org/2ze3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ze3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ze3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ze3 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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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=2ze3 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=2ze3 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 DFA0005 protein complexed with alpha-ketoglutarate (AKG) from an alkali-tolerant bacterium Deinococcus ficus has been determined to a resolution of 1.62 A. The monomer forms an incomplete alpha7/beta8 barrel with a protruding alpha8 helix that interacts extensively with another subunit to form a stable dimer of two complete alpha8/beta8 barrels. The dimer is further stabilized by four glycerol molecules situated at the interface. One unique AKG ligand binding pocket per subunit is detected. Fold match using the DALI and SSE servers identifies DFA0005 as belonging to the isocitrate lyase/phosphoenolpyruvate mutase (ICL/PEPM) superfamily. However, further detailed structural and sequence comparison with other members in this superfamily and with other families containing AKG ligand indicate that DFA0005 protein exhibits considerable distinguishing features of its own and can be considered a novel member in this ICL/PEPM superfamily. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
Crystal structure of DFA0005 complexed with alpha-ketoglutarate: A novel member of the ICL/PEPM superfamily from alkali-tolerant Deinococcus ficus.,Liao CJ, Chin KH, Lin CH, Tsai PS, Lyu PC, Young CC, Wang AH, Chou SH Proteins. 2008 Apr 23. PMID:18433062<ref>PMID:18433062</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ze3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ccug 51391]]
[[Category: Deinococcus ficus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chin, K H]]
[[Category: Chin KH]]
[[Category: Chou, S H]]
[[Category: Chou SH]]
[[Category: Liao, C J]]
[[Category: Liao CJ]]
[[Category: Alkaliphilic]]
[[Category: Alpha-ketoglutarate ligand]]
[[Category: Deinococcus ficus]]
[[Category: Icl/pepm superfamily]]
[[Category: Isomerase]]
[[Category: Organic waste left-over decomposition]]

Latest revision as of 13:57, 13 March 2024

Crystal Structure of DFA0005 Complexed with alpha-Ketoglutarate: A Novel Member of the ICL/PEPM Superfamily from Alkali-tolerant Deinococcus ficus

2ze3, resolution 1.65Å

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