2hp3: Difference between revisions

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-[[Image:2hp3.png|left|200px]]
-{{STRUCTURE_2hp3|  PDB=2hp3  |  SCENE=  }}
+==Crystal structure of iminodisuccinate epimerase==
+<StructureSection load='2hp3' size='340' side='right'caption='[[2hp3]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2hp3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HP3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.71&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=2hp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp3 OCA], [https://pdbe.org/2hp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hp3 RCSB], [https://www.ebi.ac.uk/pdbsum/2hp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hp3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q1L4E3_RHIRD Q1L4E3_RHIRD]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/2hp3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2hp3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Iminodisuccinate (IDS) epimerase catalyzes the epimerisation of R,R-, S,S- and R,S- iminodisuccinate, one step in the biodegradation of the chelating agent iminodisuccinate by Agrobacterium tumefaciens BY6. The enzyme is a member of the MmgE/PrpD protein family, a diverse and little characterized class of proteins of prokaryotic and eukaryotic origin. IDS epimerase does not show significant overall amino acid sequence similarity to any other protein of known three-dimensional structure. The crystal structure of this novel epimerase has been determined by multi-wavelength diffraction to 1.5 A resolution using selenomethionine-substituted enzyme. In the crystal, the enzyme forms a homo-dimer, and the subunit consists of two domains. The larger domain, not consecutive in sequence and comprising residues Met1-Lys266 and Leu400-Pro446, forms a novel all alpha-helical fold with a central six-helical bundle. The second, smaller domain folds into an alpha+beta domain, related in topology to chorismate mutase by a circular permutation. IDS epimerase is thus not related in three-dimensional structure to other known epimerases. The fold of the IDS epimerase is representative for the whole MmgE/PrpD family. The putative active site is located at the interface between the two domains of the subunit, and is characterized by a positively charged surface, consistent with the binding of a highly negatively charged substrate such as iminodisuccinate. Docking experiments suggest a two-base mechanism for the epimerisation reaction.
-===Crystal structure of iminodisuccinate epimerase===
+Three-dimensional structure of iminodisuccinate epimerase defines the fold of the MmgE/PrpD protein family.,Lohkamp B, Bauerle B, Rieger PG, Schneider G J Mol Biol. 2006 Sep 22;362(3):555-66. Epub 2006 Jul 29. PMID:16934291<ref>PMID:16934291</ref>
-{{ABSTRACT_PUBMED_16934291}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2hp3" style="background-color:#fffaf0;"></div>
-[[2hp3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HP3 OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:016934291</ref><references group="xtra"/>
+</StructureSection>
 [[Category: Agrobacterium tumefaciens]]
-[[Category: Bauerle, B.]]
+[[Category: Large Structures]]
-[[Category: Lohkamp, B.]]
+[[Category: Bauerle B]]
-[[Category: Rieger, P G.]]
+[[Category: Lohkamp B]]
-[[Category: Schneider, G.]]
+[[Category: Rieger PG]]
-[[Category: 6 helix bundle]]
+[[Category: Schneider G]]
-[[Category: Chorismate mutase like]]
-[[Category: Isomerase]]
-[[Category: Mmge/prpd fold]]