Journal article
The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti
Elise M Laming, Aaron P McGrath, J Mitchell Guss, Ulrike Kappler, Megan J Maher
JOURNAL OF INORGANIC BIOCHEMISTRY | ELSEVIER SCIENCE INC | Published : 2012
Abstract
The X-ray crystal structure of oxidised pseudoazurin from the denitrifying plant symbiotic bacterium Sinorhizobium meliloti (SmPAz2) has been solved to a resolution of 2.0 Å. The pseudoazurin from Sinorhizobium sp. is unusual as it forms an operon with a sulfite dehydrogenase enzyme, rather than a Cu nitrite reductase. Examination of the structure reveals that the geometric parameters of the Type I Cu site in SmPAz2 correlate with observed features in the electronic spectrum of the protein. Comparison of the structure of SmPAz2 with those of pseudoazurins from five other bacterial species shows that the surface of SmPAz2 bears a conserved hydrophobic patch encircled by positively-charged res..
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Awarded by Australian Research Council
Funding Acknowledgements
We thank Dr Miriam-Rose Ash for her careful reading of the manuscript. This study was supported by the ARC fellowship and grant (DP0878525) to UK. This research was undertaken on the MX1 and MX2 beamlines at the Australian Synchrotron, Victoria, Australia. M.J.M. is supported by a LIMS Senior Research Fellowship.