Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The crystal structure of pseudoazurin from Methylobacterium extorquens AM1 (PAZAM1) has been solved by the molecular replacement method using copper-copper distances as translation parameters, which were obtained from difference Patterson maps calculated with the synchrotron radiation data containing the multiwavelength anomalous-dispersion effect. The structure refinement was carried out by the use of molecular dynamics optimization and the restrained least-squares method. The final crystallographic R factor was 19.9% for the 14 365 reflections greater than 3sigma between 1.5 and 8.0 A resolution. This report describes the characteristic features of the structure of PAZAM 1 as well as the effectiveness of synchrotron radiation for structure analysis of metalloproteins. The environment of the metal active site and the structural differences among blue-copper proteins are discussed.
Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 A resolution.,Inoue T, Kai Y, Harada S, Kasai N, Ohshiro Y, Suzuki S, Kohzuma T, Tobari J Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):317-28. PMID:15299445[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Inoue T, Kai Y, Harada S, Kasai N, Ohshiro Y, Suzuki S, Kohzuma T, Tobari J. Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 A resolution. Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):317-28. PMID:15299445 doi:10.1107/S0907444994000260
