3qhb: Difference between revisions
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New page: '''Unreleased structure''' The entry 3qhb is ON HOLD Authors: Cooley, R.B., Arp, D.J., Karplus, P.A. Description: Crystal structure of oxidized Symerythrin from Cyanophora paradoxa |
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==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]] | |||
Latest revision as of 02:18, 21 November 2024
Crystal structure of oxidized Symerythrin from Cyanophora paradoxa
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