3qhb: Difference between revisions
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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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QHB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qhc|3qhc]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF180 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2762 Cyanophora paradoxa])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qhb RCSB], [http://www.ebi.ac.uk/pdbsum/3qhb PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cyanophora paradoxa]] | [[Category: Cyanophora paradoxa]] | ||
[[Category: Arp, D J | [[Category: Arp, D J]] | ||
[[Category: Cooley, R B | [[Category: Cooley, R B]] | ||
[[Category: Karplus, P A | [[Category: Karplus, P A]] | ||
[[Category: Carboxylate bridged-diiron]] | [[Category: Carboxylate bridged-diiron]] | ||
[[Category: Ferritin-like superfamily]] | [[Category: Ferritin-like superfamily]] | ||
[[Category: Four-helix bundle]] | [[Category: Four-helix bundle]] | ||
[[Category: Metal transport]] | [[Category: Metal transport]] | ||
Revision as of 10:45, 19 December 2014
Crystal structure of oxidized Symerythrin from Cyanophora paradoxa
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