3e1t: Difference between revisions

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 <StructureSection load='3e1t' size='340' side='right'caption='[[3e1t]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3e1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"myxobotrys_variabilis"_zukal_1896 "myxobotrys variabilis" zukal 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3e1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chondromyces_crocatus Chondromyces crocatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1T FirstGlance]. <br>
-</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.05&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cndh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=52 "Myxobotrys variabilis" Zukal 1896])</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=3e1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1t OCA], [https://pdbe.org/3e1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1t RCSB], [https://www.ebi.ac.uk/pdbsum/3e1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1t ProSAT]</span></td></tr>
 </table>
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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=3e1t ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of the FAD-dependent chondrochloren halogenase CndH has been established at 2.1 A resolution. The enzyme contains the characteristic FAD-binding scaffold of the glutathione reductase superfamily. Except for its C-terminal domain, the chainfold of CndH is virtually identical with those of FAD-dependent aromatic hydroxylases. When compared to the structurally known FAD-dependent halogenases PrnA and RebH, CndH lacks a 45 residue segment near position 100 and deviates in the C-terminal domain. Both variations are near the active center and appear to reflect substrate differences. Whereas PrnA and RebH modify free tryptophan, CndH halogenates the tyrosyl group of a chondrochloren precursor that is most likely bound to a carrier protein. In contrast to PrnA and RebH, which enclose their small substrate completely, CndH has a large non-polar surface patch that may accommodate the putative carrier. Apart from the substrate binding site, the active center of CndH corresponds to those of PrnA and RebH. At the halogenation site, CndH has the characteristic lysine (Lys76) but lacks the required base Glu346 (PrnA). This base may be supplied by a residue of its C-terminal domain or by the carrier. These differences were corroborated by an overall sequence comparison between the known FAD-dependent halogenases, which revealed a split into a PrnA-RebH group and a CndH group. The two functionally established members of the CndH group use carrier-bound substrates, whereas three members of PrnA-RebH group are known to accept a free amino acid. Given the structural and functional distinction, we classify CndH as a new variant B of the FAD-dependent halogenases, adding a new feature to the structurally established variant A enzymes PrnA and RebH.
-Structure and action of the myxobacterial chondrochloren halogenase CndH: a new variant of FAD-dependent halogenases.,Buedenbender S, Rachid S, Muller R, Schulz GE J Mol Biol. 2009 Jan 16;385(2):520-30. Epub 2008 Oct 30. PMID:19000696<ref>PMID:19000696</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3e1t" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Myxobotrys variabilis zukal 1896]]
+[[Category: Chondromyces crocatus]]
 [[Category: Large Structures]]
-[[Category: Buedenbender, S]]
+[[Category: Buedenbender S]]
-[[Category: Mueller, R]]
+[[Category: Mueller R]]
-[[Category: Rachid, S]]
+[[Category: Rachid S]]
-[[Category: Schulz, G E]]
+[[Category: Schulz GE]]
-[[Category: Fad dependent halogenase]]
-[[Category: Flavoprotein]]