1s6l: Difference between revisions

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[[Image:1s6l.gif|left|200px]]
[[Image:1s6l.gif|left|200px]]


{{Structure
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|PDB= 1s6l |SIZE=350|CAPTION= <scene name='initialview01'>1s6l</scene>
The line below this paragraph, containing "STRUCTURE_1s6l", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE= MERB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
{{STRUCTURE_1s6l|  PDB=1s6l |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6l OCA], [http://www.ebi.ac.uk/pdbsum/1s6l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s6l RCSB]</span>
}}


'''Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system'''
'''Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system'''
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[[Category: Summers, A O.]]
[[Category: Summers, A O.]]
[[Category: Valafar, H.]]
[[Category: Valafar, H.]]
[[Category: lyase]]
[[Category: Lyase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:21:48 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:38:08 2008''

Revision as of 08:21, 3 May 2008

File:1s6l.gif

Template:STRUCTURE 1s6l

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


OverviewOverview

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 StructureAbout this Structure

1S6L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 08:21:48 2008

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