3qhb: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/YCX8_CYAPA YCX8_CYAPA]  
[https://www.uniprot.org/uniprot/YCX8_CYAPA YCX8_CYAPA]  
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 02:18, 21 November 2024

Crystal structure of oxidized Symerythrin from Cyanophora paradoxa

3qhb, resolution 1.20Å

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