3u25

Crystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pairCrystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pair

Structural highlights 3u25 is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.18Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. Publication Abstract from PubMed Redox reactions of tyrosine play key roles in many biological processes, including water oxidation and DNA synthesis. We first review the redox properties of tyrosine (and other phenols) in small molecules and related polypeptides, then report work on (H20)/(Y48)-modified Pseudomonas aeruginosa azurin. The crystal structure of this protein (1.18A resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8A tyrosine-O to histidine-N distance). A firm conclusion is that proper tuning of the tyrosine potential by a proton-accepting base is critical for biological redox functions. Redox properties of tyrosine and related molecules.,Warren JJ, Winkler JR, Gray HB FEBS Lett. 2012 Mar 9;586(5):596-602. Epub 2011 Dec 26. PMID:22210190 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Azurin 3D structures

spinqualitylabelsall models 3u25, resolution 1.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image