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1s6l

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(New page: 200px<br /><applet load="1s6l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s6l" /> '''Solution structure of MerB, the Organomercur...)
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Revision as of 00:02, 21 November 2007

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1s6l

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Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system

Overview

Mercury resistant bacteria have developed a system of two enzymes (MerA, and MerB), which allows them to efficiently detoxify both ionic and, organomercurial compounds. The organomercurial lyase (MerB) catalyzes the, protonolysis of the carbon-mercury bond resulting in the formation of, ionic mercury and a reduced hydrocarbon. The ionic mercury [Hg(II)] is, subsequently reduced to the less reactive elemental mercury [Hg(0)] by a, specific mercuric reductase (MerA). To better understand MerB's unique, enzymatic activity, we used nuclear magnetic resonance (NMR) spectroscopy, to determine the structure of the free enzyme. MerB is characterized by a, novel protein fold consisting of three noninteracting antiparallel, beta-sheets surrounded by six alpha-helices. By comparing the NMR data of, free MerB and the MerB/Hg/DTT complex, we identified a set of residues, that likely define a Hg/DTT binding site. These residues cluster around, two cysteines (C(96) and C(159)) that are crucial to MerB's catalytic, activity. A detailed analysis of the structure revealed the presence of an, extensive hydrophobic groove adjacent to this Hg/DTT binding site. This, extensive hydrophobic groove has the potential to interact with the, hydrocarbon moiety of a wide variety of substrates and may explain the, broad substrate specificity of MerB.

About this Structure

1S6L is a Single protein structure of sequence from Escherichia coli. Active as Alkylmercury lyase, with EC number 4.99.1.2 Full crystallographic information is available from OCA.

Reference

NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system., Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG, Biochemistry. 2004 Jul 6;43(26):8322-32. PMID:15222745

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