1s6l: Difference between revisions
New page: left|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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'''Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system'''<br /> | '''Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system'''<br /> | ||
==Overview== | ==Overview== | ||
Mercury resistant bacteria have developed a system of two enzymes (MerA | 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== | ==About this Structure== | ||
1S6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Alkylmercury_lyase Alkylmercury lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.2 4.99.1.2] Full crystallographic information is available from [http:// | 1S6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Alkylmercury_lyase Alkylmercury lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.2 4.99.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6L OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Benison, G | [[Category: Benison, G C.]] | ||
[[Category: Legault, P.]] | [[Category: Legault, P.]] | ||
[[Category: Lello, P | [[Category: Lello, P Di.]] | ||
[[Category: Omichinski, J | [[Category: Omichinski, J G.]] | ||
[[Category: Pitts, K | [[Category: Pitts, K E.]] | ||
[[Category: Summers, A | [[Category: Summers, A O.]] | ||
[[Category: Valafar, H.]] | [[Category: Valafar, H.]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:30 2008'' | ||
