3qhb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of oxidized Symerythrin from Cyanophora paradoxa== | |
| + | <StructureSection load='3qhb' size='340' side='right'caption='[[3qhb]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qhb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanophora_paradoxa Cyanophora paradoxa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHB 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]] 1.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=3qhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhb OCA], [https://pdbe.org/3qhb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qhb RCSB], [https://www.ebi.ac.uk/pdbsum/3qhb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/YCX8_CYAPA YCX8_CYAPA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | All known internal covalent cross-links in proteins involve functionalized groups having oxygen, nitrogen, or sulfur atoms present to facilitate their formation. Here, we report a carbon-carbon cross-link between two unfunctionalized side chains. This valine-phenyalanine cross-link, produced in an oxygen-dependent reaction, is generated by its own carboxylate-bridged diiron center and serves to stabilize the metallocenter. This finding opens the door to new types of posttranslational modifications, and it demonstrates new catalytic potential of diiron centers. | ||
| - | + | A diiron protein autogenerates a valine-phenylalanine cross-link.,Cooley RB, Rhoads TW, Arp DJ, Karplus PA Science. 2011 May 20;332(6032):929. PMID:21596985<ref>PMID:21596985</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3qhb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cyanophora paradoxa]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arp DJ]] | ||
| + | [[Category: Cooley RB]] | ||
| + | [[Category: Karplus PA]] | ||
Current revision
Crystal structure of oxidized Symerythrin from Cyanophora paradoxa
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