6u58

<table><tr><td colspan='2'>[[6u58]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U58 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=6u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u58 OCA], [http://pdbe.org/6u58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u58 RCSB], [http://www.ebi.ac.uk/pdbsum/6u58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u58 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The amino-acid sequence of the Toho-1 beta-lactamase contains several conserved residues in the active site, including Ser70, Lys73, Ser130 and Glu166, some of which coordinate a catalytic water molecule. This catalytic water molecule is essential in the acylation and deacylation parts of the reaction mechanism through which Toho-1 inactivates specific antibiotics and provides resistance to its expressing bacterial strains. To investigate the function of Glu166 in the acylation part of the catalytic mechanism, neutron and X-ray crystallographic studies were performed on a Glu166Gln mutant. The structure of this class A beta-lactamase mutant provides several insights into its previously reported reduced drug-binding kinetic rates. A joint refinement of both X-ray and neutron diffraction data was used to study the effects of the Glu166Gln mutation on the active site of Toho-1. This structure reveals that while the Glu166Gln mutation has a somewhat limited impact on the positions of the conserved amino acids within the active site, it displaces the catalytic water molecule from the active site. These subtle changes offer a structural explanation for the previously observed decreases in the binding of non-beta-lactam inhibitors such as the recently developed diazobicyclooctane inhibitor avibactam.

 

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== References ==

[[Category: Beta-lactamase]]

[[Category: Langan, P S]]

[[Category: Sullivan, B]]

[[Category: Weiss, K L]]

[[Category: Hydrolase]]