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''' | ==Crystal Structure of p-acrylamido-phenylalanine modified TEM1 beta-lactamase from Escherichia coli :E166N mutant== | ||
<StructureSection load='4zj2' size='340' side='right' caption='[[4zj2]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zj2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZJ2 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4OV:(2R)-2-[(1R)-2-[(2S)-2-AMINO-2-CARBOXYETHOXY]-1-{[(2R)-2-AMINO-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5-METHYL-3,6-DIHYDRO-2H-1,3-THIAZINE-4-CARBOXYLIC+ACID'>4OV</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zj1|4zj1]], [[4zj3|4zj3]]</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=4zj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zj2 RCSB], [http://www.ebi.ac.uk/pdbsum/4zj2 PDBsum]</span></td></tr> | ||
[[Category: | </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: Choi, S]] | |||
[[Category: Han, G W]] | |||
[[Category: Nasertorabi, F]] | [[Category: Nasertorabi, F]] | ||
[[Category: | [[Category: Reed, S A]] | ||
[[Category: | [[Category: Schultz, P G]] | ||
[[Category: Stevens, C S]] | |||
[[Category: Xiao, H]] | [[Category: Xiao, H]] | ||
[[Category: | [[Category: Evolutionary advantage]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: Noncanonical amino acid]] | |||
[[Category: Protein evolution]] | |||
Revision as of 15:21, 20 May 2015
Crystal Structure of p-acrylamido-phenylalanine modified TEM1 beta-lactamase from Escherichia coli :E166N mutantCrystal Structure of p-acrylamido-phenylalanine modified TEM1 beta-lactamase from Escherichia coli :E166N mutant
Structural highlights
Function[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. |
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