1va0: Difference between revisions

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-[[Image:1va0.gif|left|200px]]
-<!--
+==Crystal Structure of the Native Form of Uroporphyrin III C-methyl transferase from Thermus thermophilus==
-The line below this paragraph, containing "STRUCTURE_1va0", creates the "Structure Box" on the page.
+<StructureSection load='1va0' size='340' side='right'caption='[[1va0]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1va0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-{{STRUCTURE_1va0|  PDB=1va0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1va0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va0 OCA], [https://pdbe.org/1va0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va0 RCSB], [https://www.ebi.ac.uk/pdbsum/1va0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va0 ProSAT], [https://www.topsan.org/Proteins/RSGI/1va0 TOPSAN]</span></td></tr>
+</table>
-'''Crystal Structure of the Native Form of Uroporphyrin III C-methyl transferase from Thermus thermophilus'''
+== Function ==
+[https://www.uniprot.org/uniprot/Q5SKH6_THET8 Q5SKH6_THET8]
+== Evolutionary Conservation ==
-==Overview==
+[[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/va/1va0_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=1va0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
 Uroporphyrinogen-III C-methyltransferase from Thermus thermophilus is a multifunctional protein responsible for two of the eight S-adenosyl-methionine-dependent methylations of the corrin ring during vitamin B(12) synthesis. The structure of this protein has been solved to 2.0 A resolution in both the apo and cofactor-bound form. The monomer consists of two domains, A and B, each consisting of a five-stranded beta-sheet and two or three alpha-helices, with the cofactor bound at the interface. The biological unit is the dimer found in the asymmetric unit. This dimer is related by a non-crystallographic twofold such that two B domains combine to form a long ten-stranded beta-sheet. When compared with solved related structures, this structure shows clear differences in the region involved in cofactor and substrate binding, affirming the role of several previously implicated residues and questioning others. The solved related structures are characterized by an exposed active site. The T. thermophilus structure has this site restricted by the interaction of a flexible loop structure with a highly conserved residue, suggesting a mechanistic role. This structure represents the ;closed' form of the protein.
-==About this Structure==
+Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus.,Rehse PH, Kitao T, Tahirov TH Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):913-9. Epub 2005, Jun 24. PMID:15983414<ref>PMID:15983414</ref>
-VA0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA0 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus., Rehse PH, Kitao T, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):913-9. Epub 2005, Jun 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15983414 15983414]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1va0" style="background-color:#fffaf0;"></div>
-[[Category: Thermus thermophilus]]
+== References ==
-[[Category: Uroporphyrinogen-III C-methyltransferase]]
+<references/>
-[[Category: Kitao, T.]]
+__TOC__
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+</StructureSection>
-[[Category: Rehse, P H.]]
+[[Category: Large Structures]]
-[[Category: Tahirov, T H.]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: Riken structural genomics/proteomics initiative]]
+[[Category: Kitao T]]
-[[Category: Rsgi]]
+[[Category: Rehse PH]]
-[[Category: Structural genomic]]
+[[Category: Tahirov TH]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:17:10 2008''