4rva
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for deacylation== |
| - | + | <StructureSection load='4rva' size='340' side='right' caption='[[4rva]], [[Resolution|resolution]] 1.44Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4rva]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RVA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1btl|1btl]]</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> | |
| - | [[Category: | + | <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=4rva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rva OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rva RCSB], [http://www.ebi.ac.uk/pdbsum/4rva PDBsum]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-lactamase]] | ||
| + | [[Category: Chow, D C]] | ||
[[Category: Gilbert, H]] | [[Category: Gilbert, H]] | ||
[[Category: Hu, L]] | [[Category: Hu, L]] | ||
| - | [[Category: Stojanoski, V]] | ||
| - | [[Category: Prasad, B.V.V]] | ||
[[Category: Palzkill, T]] | [[Category: Palzkill, T]] | ||
| + | [[Category: Prasad, B V.V]] | ||
[[Category: Sankaran, B]] | [[Category: Sankaran, B]] | ||
| - | [[Category: | + | [[Category: Stojanoski, V]] |
| + | [[Category: Globular]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 11:35, 4 March 2015
A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for deacylation
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Categories: Beta-lactamase | Chow, D C | Gilbert, H | Hu, L | Palzkill, T | Prasad, B V.V | Sankaran, B | Stojanoski, V | Globular | Hydrolase
