1iby
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(New page: 200px<br /><applet load="1iby" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iby, resolution 1.65Å" /> '''RED COPPER PROTEIN N...)
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Revision as of 19:37, 24 November 2007
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RED COPPER PROTEIN NITROSOCYANIN FROM NITROSOMONAS EUROPAEA
Overview
Nitrosocyanin (NC) is a mononuclear red copper protein isolated from the, ammonia oxidizing bacterium Nitrosomonas europaea. Although NC exhibits, some sequence homology to classic blue copper proteins, its spectroscopic, and electrochemical properties are drastically different. The 1.65 A, resolution crystal structure of oxidized NC reveals an unprecedented, trimer of single domain cupredoxins. Each copper center is partially, covered by an unusual extended beta-hairpin structure from an adjacent, monomer. The copper ion is coordinated by His 98, His 103, Cys 95, a, single side chain oxygen of Glu 60, and a solvent molecule. In the 2.3 A, resolution structure of reduced NC, His 98 shifts away from the copper, ion, and the solvent molecule is not observed. The arrangement of these, ligands renders the coordination geometry of the NC red copper center, distinct from that of blue copper centers. In particular, the red copper, center has a higher coordination number and lacks the long Cu-S(Met) and, short Cu-S(Cys) bond distances characteristic of blue copper. Moreover, the red copper center is square pyramidal whereas blue copper is typically, distorted tetrahedral. Analysis of the NC structure provides insight into, possible functions of this new type of biological copper center.
About this Structure
1IBY is a Single protein structure of sequence from Nitrosomonas europaea with CU and HEZ as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel red copper protein from Nitrosomonas europaea., Lieberman RL, Arciero DM, Hooper AB, Rosenzweig AC, Biochemistry. 2001 May 15;40(19):5674-81. PMID:11341832
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