4j5f: Difference between revisions
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==Crystal Structure of B. thuringiensis AiiA mutant F107W== | |||
=== | <StructureSection load='4j5f' size='340' side='right' caption='[[4j5f]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4j5f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J5F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J5F FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5h|4j5h]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aiiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1428 Bacillus thuringiensis])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quorum-quenching_N-acyl-homoserine_lactonase Quorum-quenching N-acyl-homoserine lactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.81 3.1.1.81] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j5f RCSB], [http://www.ebi.ac.uk/pdbsum/4j5f PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Autoinducer inactivator A (AiiA) is a metal-dependent N-acyl homoserine lactone hydrolase that displays broad substrate specificity but shows a preference for substrates with long N-acyl substitutions. Previously, crystal structures of AiiA in complex with the ring-opened product N-hexanoyl-l-homoserine revealed binding interactions near the metal center but did not identify a binding pocket for the N-acyl chains of longer substrates. Here we report the crystal structure of an AiiA mutant, F107W, determined in the presence and absence of N-decanoyl-l-homoserine. F107 is located in a hydrophobic cavity adjacent to the previously identified ligand binding pocket, and the F107W mutation results in the formation of an unexpected interaction with the ring-opened product. Notably, the structure reveals a previously unidentified hydrophobic binding pocket for the substrate's N-acyl chain. Two aromatic residues, F64 and F68, form a hydrophobic clamp, centered around the seventh carbon in the product-bound structure's decanoyl chain, making an interaction that would also be available for longer substrates, but not for shorter substrates. Steady-state kinetics using substrates of various lengths with AiiA bearing mutations at the hydrophobic clamp, including insertion of a redox-sensitive cysteine pair, confirms the importance of this hydrophobic feature for substrate preference. Identifying the specificity determinants of AiiA will aid the development of more selective quorum-quenching enzymes as tools and as potential therapeutics. | |||
A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis.,Liu CF, Liu D, Momb J, Thomas PW, Lajoie A, Petsko GA, Fast W, Ringe D Biochemistry. 2013 Mar 5;52(9):1603-10. doi: 10.1021/bi400050j. Epub 2013 Feb 20. PMID:23387521<ref>PMID:23387521</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus thuringiensis]] | [[Category: Bacillus thuringiensis]] | ||
[[Category: Quorum-quenching N-acyl-homoserine lactonase]] | [[Category: Quorum-quenching N-acyl-homoserine lactonase]] | ||
[[Category: Fast, W | [[Category: Fast, W]] | ||
[[Category: Lajoie, A | [[Category: Lajoie, A]] | ||
[[Category: Liu, C F | [[Category: Liu, C F]] | ||
[[Category: Liu, D | [[Category: Liu, D]] | ||
[[Category: Momb, J | [[Category: Momb, J]] | ||
[[Category: Petsko, G A | [[Category: Petsko, G A]] | ||
[[Category: Ringe, D | [[Category: Ringe, D]] | ||
[[Category: Thomas, P W | [[Category: Thomas, P W]] | ||
[[Category: Aiia]] | [[Category: Aiia]] | ||
[[Category: Beta-hairpin loop]] | [[Category: Beta-hairpin loop]] | ||
