3U25

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

Summary for 3U25

• Entry DOI: 10.2210/pdb3u25/pdb
• Descriptor: Azurin, COPPER (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: azurin, cupredoxin, electron transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 2
• Total formula weight: 28092.73

Authors

Warren, J.J.,Winkler, J.R.,Gray, H.B. (deposition date: 2011-09-30, release date: 2011-12-28, Last modification date: 2024-10-16)

Primary citation

Warren, J.J.,Winkler, J.R.,Gray, H.B.
Redox properties of tyrosine and related molecules.
Febs Lett., 586:596-602, 2012

PubMed Abstract: 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 (1.18Å resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8Å 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.

PubMed: 22210190
DOI: 10.1016/j.febslet.2011.12.014

Experimental method

X-RAY DIFFRACTION (1.18 Å)