3qhb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (02:18, 21 November 2024) (edit) (undo)
 
Line 10: Line 10:
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/YCX8_CYAPA YCX8_CYAPA]
[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&reg;/PubMed&reg;, 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__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of oxidized Symerythrin from Cyanophora paradoxa

PDB ID 3qhb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools