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| <StructureSection load='3sbl' size='340' side='right'caption='[[3sbl]], [[Resolution|resolution]] 2.31Å' scene=''> | | <StructureSection load='3sbl' size='340' side='right'caption='[[3sbl]], [[Resolution|resolution]] 2.31Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3sbl]] is a 1 chain structure with sequence from [https://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=3SBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBL FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3sbl]] 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=3SBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBL FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 2.31Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rkj|3rkj]], [[3rkk|3rkk]]</div></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaNDM-1 ([https://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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbl OCA], [https://pdbe.org/3sbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbl RCSB], [https://www.ebi.ac.uk/pdbsum/3sbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbl ProSAT]</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=3sbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbl OCA], [https://pdbe.org/3sbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbl RCSB], [https://www.ebi.ac.uk/pdbsum/3sbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbl ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/BLAN1_KLEPN BLAN1_KLEPN]] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
| | [https://www.uniprot.org/uniprot/BLAN1_KLEPN BLAN1_KLEPN] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The New Delhi Metallo-beta-lactamase (NDM-1) gene makes multiple pathogenic microorganisms resistant to all known beta-lactam antibiotics. The rapid emergence of NDM-1 has been linked to mobile plasmids that move between different strains resulting in world-wide dissemination. Biochemical studies revealed that NDM-1 is capable of efficiently hydrolyzing a wide range of beta-lactams, including many carbapenems considered as "last resort" antibiotics. The crystal structures of metal-free apo- and monozinc forms of NDM-1 presented here revealed an enlarged and flexible active site of class B1 metallo-beta-lactamase. This site is capable of accommodating many beta-lactam substrates by having many of the catalytic residues on flexible loops, which explains the observed extended spectrum activity of this zinc dependent beta-lactamase. Indeed, five loops contribute "keg" residues in the active site including side chains involved in metal binding. Loop 1 in particular, shows conformational flexibility, apparently related to the acceptance and positioning of substrates for cleavage by a zinc-activated water molecule.
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| Structure of apo- and monometalated forms of NDM-1--a highly potent carbapenem-hydrolyzing metallo-beta-lactamase.,Kim Y, Tesar C, Mire J, Jedrzejczak R, Binkowski A, Babnigg G, Sacchettini J, Joachimiak A PLoS One. 2011;6(9):e24621. Epub 2011 Sep 8. PMID:21931780<ref>PMID:21931780</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3sbl" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Beta-lactamase]] | | [[Category: Klebsiella pneumoniae]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Babnigg, J]] | | [[Category: Babnigg J]] |
| [[Category: Binkowski, T A]] | | [[Category: Binkowski TA]] |
| [[Category: Jedrzejczak, R]] | | [[Category: Jedrzejczak R]] |
| [[Category: Joachimiak, A]] | | [[Category: Joachimiak A]] |
| [[Category: Kim, Y]] | | [[Category: Kim Y]] |
| [[Category: Structural genomic]]
| | [[Category: Mire J]] |
| [[Category: MTBI, Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors]]
| | [[Category: Sacchettini J]] |
| [[Category: Mire, J]] | | [[Category: Tesar C]] |
| [[Category: Sacchettini, J]] | |
| [[Category: Tesar, C]] | |
| [[Category: Alpha-beta structure]]
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| [[Category: Hydrolase]]
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| [[Category: Mcsg]]
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| [[Category: Mtbi]]
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| [[Category: Psi-biology]]
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| [[Category: Structures of mtb proteins conferring susceptibility to known mtb inhibitor]]
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