A Diiron Protein Autogenerates a Valine-Phenylalanine Cross-Link

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 o...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2011-05, Vol.332 (6032), p.929-929
Main Authors: Cooley, Richard B., Rhoads, Timothy W., Arp, Daniel J., Karplus, P. Andrew
Format: Article
Language:English
Subjects:
Amino acids
Atoms
Binding Sites
Biological and medical sciences
BREVIA
Carbon
Carbon-carbon composites
Catalysis
Catalysts
Chemical bonds
Covalence
Crosslinking
Crystalline structure
Crystallography, X-Ray
Cyanophora - chemistry
Cyanophora - metabolism
Doors
Fundamental and applied biological sciences. Psychology
Iron
Iron - chemistry
Metalloproteins - chemistry
Metalloproteins - metabolism
Molecular biophysics
Oxygen
Oxygen - chemistry
Phenylalanine - chemistry
Plant Proteins - chemistry
Plant Proteins - metabolism
Polymers
Protein Conformation
Protein Structure, Secondary
Proteins
Structure in molecular biology
Sulfur
Valine - chemistry
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1205687