1fc5: Difference between revisions

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-{{Seed}}
-[[Image:1fc5.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN==
-The line below this paragraph, containing "STRUCTURE_1fc5", creates the "Structure Box" on the page.
+<StructureSection load='1fc5' size='340' side='right'caption='[[1fc5]], [[Resolution|resolution]] 2.20&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'>[[1fc5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FC5 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]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_1fc5|  PDB=1fc5  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fc5 OCA], [https://pdbe.org/1fc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fc5 ProSAT], [https://www.topsan.org/Proteins/BSGI/1fc5 TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MOEA_ECOLI MOEA_ECOLI] Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.<ref>PMID:15632135</ref>
+== 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/fc/1fc5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fc5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions.
-===CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN===
+The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.,Schrag JD, Huang W, Sivaraman J, Smith C, Plamondon J, Larocque R, Matte A, Cygler M J Mol Biol. 2001 Jul 6;310(2):419-31. PMID:11428898<ref>PMID:11428898</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11428898}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1fc5" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11428898 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11428898}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FC5 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC5 OCA].
-==Reference==
-<ref group="xtra">PMID:11428898</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
+[[Category: Large Structures]]
-[[Category: Cygler, M.]]
+[[Category: Cygler M]]
-[[Category: Huang, W.]]
+[[Category: Huang W]]
-[[Category: Bsgi]]
-[[Category: Four module]]
-[[Category: Molybdopterin]]
-[[Category: Montreal-kingston bacterial structural genomics initiative]]
-[[Category: Structural genomic]]
-[[Category: With magnesium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:45:13 2009''