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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
2008-7-16
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pubmed:databankReference |
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pubmed:abstractText |
Enzymes capable of hydrolyzing N-acyl- l-homoserine lactones (AHLs) used in some bacterial quorum-sensing pathways are of considerable interest for their ability to block undesirable phenotypes. Most known AHL hydrolases that catalyze ring opening (AHL lactonases) are members of the metallo-beta-lactamase enzyme superfamily and rely on a dinuclear zinc site for catalysis and stability. Here we report the three-dimensional structures of three product complexes formed with the AHL lactonase from Bacillus thuringiensis. Structures of the lactonase bound with two different concentrations of the ring-opened product of N-hexanoyl- l-homoserine lactone are determined at 0.95 and 1.4 A resolution and exhibit different product configurations. A structure of the ring-opened product of the non-natural N-hexanoyl- l-homocysteine thiolactone at 1.3 A resolution is also determined. On the basis of these product-bound structures, a substrate-binding model is presented that differs from previous proposals. Additionally, the proximity of the product to active-site residues and observed changes in protein conformation and metal coordination provide insight into the catalytic mechanism of this quorum-quenching metalloenzyme.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-10545172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-10757977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-11063572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-11471246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-11513844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-12507470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-12824483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-14734559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-15264254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-15271998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-15588826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-15779910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-15895999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-15908436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-16087890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-16218639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-16314577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-16684886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-16937423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-16972128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-17042472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-17073460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-17360275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-17426028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-17900178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-17999929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-18052346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-18627130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18627129-7906142
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1520-4995
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
22
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7706-14
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2008
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pubmed:articleTitle |
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.
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pubmed:affiliation |
Department of Chemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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