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| | <StructureSection load='6k9t' size='340' side='right'caption='[[6k9t]], [[Resolution|resolution]] 1.46Å' scene=''> | | <StructureSection load='6k9t' size='340' side='right'caption='[[6k9t]], [[Resolution|resolution]] 1.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k9t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K9T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k9t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K9T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CEF:CEFOTAXIME,+C3+CLEAVED,+OPEN,+BOUND+FORM'>CEF</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.459Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bla-ACC-1, acc-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CEF:CEFOTAXIME,+C3+CLEAVED,+OPEN,+BOUND+FORM'>CEF</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'>[https://proteopedia.org/fgij/fg.htm?mol=6k9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k9t OCA], [https://pdbe.org/6k9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k9t RCSB], [https://www.ebi.ac.uk/pdbsum/6k9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k9t 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=6k9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k9t OCA], [http://pdbe.org/6k9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k9t RCSB], [http://www.ebi.ac.uk/pdbsum/6k9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k9t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q9XB24_KLEPN Q9XB24_KLEPN] |
| - | ACC-1 is a plasmid-encoded class C beta-lactamase identified in clinical isolates of Klebsiella pneumoniae, Proteus mirabilis, Salmonella enterica, and Escherichia coli ACC-1-producing bacteria are susceptible to cefoxitin whereas they are resistant to oxyimino cephalosporins. Here, we depict crystal structures of apo ACC-1, adenylylated ACC-1, and acylated ACC-1 complexed with cefotaxime and cefoxitin. ACC-1 has noteworthy structural alterations in the R2-loop, the Omega- loop, and the Phe119-loop along the active-site rim. The adenylate covalently bonded to the nucleophilic serine reveals a tetrahedral phosphorus mimicking the deacylation transition state. Cefotaxime in ACC-1 has a proper conformation for the substrate-assisted catalysis in that its C4 carboxylate and N5 nitrogen are adequately located to facilitate the deacylation reaction. In contrast, cefoxitin in ACC-1 has a distinct conformation in which those functional groups cannot contribute to catalysis. Furthermore, the orientation of the deacylating water relative to the acyl carbonyl group in ACC-1 is unfavorable for nucleophilic attack.
| + | |
| | | | |
| - | Structural insights into catalytic relevances of substrates' poses in ACC-1.,Bae DW, Jung YE, An YJ, Na JH, Cha SS Antimicrob Agents Chemother. 2019 Aug 26. pii: AAC.01411-19. doi:, 10.1128/AAC.01411-19. PMID:31451494<ref>PMID:31451494</ref>
| + | ==See Also== |
| - | | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6k9t" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | + | [[Category: Klebsiella pneumoniae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: An, Y J]] | + | [[Category: An YJ]] |
| - | [[Category: Bae, D W]] | + | [[Category: Bae DW]] |
| - | [[Category: Cha, S S]] | + | [[Category: Cha SS]] |
| - | [[Category: Jung, Y E]] | + | [[Category: Jung YE]] |
| - | [[Category: Na, J H]] | + | [[Category: Na JH]] |
| - | [[Category: Acc-1 class c beta-lactamase]]
| + | |
| - | [[Category: Acyl-enzyme complex]]
| + | |
| - | [[Category: Cefotaxime]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
