Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cooley RB, Rhoads TW, Arp DJ, Karplus PA. A diiron protein autogenerates a valine-phenylalanine cross-link. Science. 2011 May 20;332(6032):929. PMID:21596985 doi:10.1126/science.1205687
