5zqb
From Proteopedia
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<StructureSection load='5zqb' size='340' side='right' caption='[[5zqb]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5zqb' size='340' side='right' caption='[[5zqb]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zqb]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZQB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zqb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZQB 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=PNM:OPEN+FORM+-+PENICILLIN+G'>PNM</scene></td></tr> | </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=PNM:OPEN+FORM+-+PENICILLIN+G'>PNM</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmo2812 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</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=5zqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqb OCA], [http://pdbe.org/5zqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zqb RCSB], [http://www.ebi.ac.uk/pdbsum/5zqb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqb ProSAT]</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=5zqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqb OCA], [http://pdbe.org/5zqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zqb RCSB], [http://www.ebi.ac.uk/pdbsum/5zqb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | beta-lactam antibiotics that inhibit penicillin-binding proteins (PBPs) have been widely used in the treatment of bacterial infections. However, the molecular basis underlying the different inhibitory potencies of beta-lactams against specific PBPs is not fully understood. Here, we present the crystal structures of PBPD2 from Listeria monocytogenes, a Gram-positive food-borne bacterial pathogen that causes listeriosis in humans. The acylated structures in complex with four antibiotics (penicillin G, ampicillin, cefotaxime, and cefuroxime) revealed that the beta-lactam core structures were recognized by a common set of residues; however, the R1 side chains of each antibiotic participate in different interactions with PBPD2. In addition, the structural complementarities between the side chains of beta-lactams and the enzyme were found to be highly correlated with the relative reactivities of penam or cephem antibiotics against PBPD2. Our study provides the structural basis for the inhibition of PBPD2 by clinically important beta-lactam antibiotics that are commonly used in listeriosis treatment. Our findings imply that the modification of beta-lactam side chains based on structural complementarity could be useful for the development of potent inhibitors against beta-lactam-resistant PBPs. | ||
| + | |||
| + | Crystal structures of penicillin-binding protein D2 from Listeria monocytogenes: Structural basis for antibiotic specificity.,Jeong JH, Cha HJ, Kim YG Antimicrob Agents Chemother. 2018 Aug 6. pii: AAC.00796-18. doi:, 10.1128/AAC.00796-18. PMID:30082290<ref>PMID:30082290</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zqb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Lismo]] | ||
[[Category: Jeong, J H]] | [[Category: Jeong, J H]] | ||
[[Category: Kim, Y G]] | [[Category: Kim, Y G]] | ||
Revision as of 06:30, 22 August 2018
Crystal Structure of Penicillin-Binding Protein D2 from Listeria monocytogenes in the Penicillin G bound form
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