5paz
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(New page: 200px<br /> <applet load="5paz" size="450" color="white" frame="true" align="right" spinBox="true" caption="5paz, resolution 1.76Å" /> '''REDUCED MUTANT P80A...)
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Revision as of 17:03, 29 October 2007
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REDUCED MUTANT P80A PSEUDOAZURIN FROM A. FAECALIS
Overview
In order to understand the origins of differences in redox potentials, among cupredoxins (small blue type I copper-containing proteins that, reversibly change oxidation state and interact with redox partners), we, have determined the structures of the native and two mutants (P80A and, P80I) of pseudoazurin from Alcaligenes faecalis S-6 in oxidized and, reduced forms at resolutions of 2.2 A in the worst case and 1.6 A in the, best case. The P80A mutation creates a surface pocket filled by a new, water molecule, whereas the P80I mutant excludes this water. Distinct, patterns of change occur in response to reduction for all three molecules:, the copper position shifts, Met 7 and Pro 35 move, and the relative, orientations of residues 81 to 16, 18 to the amide planes of 77 and 86, all change. ... [(full description)]
About this Structure
5PAZ is a [Single protein] structure of sequence from [Alcaligenes faecalis] with CU as [ligand]. Full crystallographic information is available from [OCA].
Reference
Site-directed mutants of pseudoazurin: explanation of increased redox potentials from X-ray structures and from calculation of redox potential differences., Libeu CA, Kukimoto M, Nishiyama M, Horinouchi S, Adman ET, Biochemistry. 1997 Oct 28;36(43):13160-79. PMID:9341204
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