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3sbl
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| - | [[ | + | ==Crystal Structure of New Delhi Metal-beta-lactamase-1 from Klebsiella pneumoniae== |
| + | <StructureSection load='3sbl' size='340' side='right' caption='[[3sbl]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3sbl]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SBL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rkj|3rkj]], [[3rkk|3rkk]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaNDM-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 Klebsiella pneumoniae])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sbl RCSB], [http://www.ebi.ac.uk/pdbsum/3sbl PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase|Beta-lactamase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
| - | [[Category: Babnigg, J | + | [[Category: Babnigg, J]] |
| - | [[Category: Binkowski, T A | + | [[Category: Binkowski, T A]] |
| - | [[Category: Jedrzejczak, R | + | [[Category: Jedrzejczak, R]] |
| - | [[Category: Joachimiak, A | + | [[Category: Joachimiak, A]] |
| - | [[Category: Kim, Y | + | [[Category: Kim, Y]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: MTBI, Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors | + | [[Category: MTBI, Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors]] |
| - | [[Category: Mire, J | + | [[Category: Mire, J]] |
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J]] |
| - | [[Category: Tesar, C | + | [[Category: Tesar, C]] |
[[Category: Alpha-beta structure]] | [[Category: Alpha-beta structure]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
| - | [[Category: Midwest center for structural genomic]] | ||
[[Category: Mtbi]] | [[Category: Mtbi]] | ||
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Structures of mtb proteins conferring susceptibility to known mtb inhibitor]] | [[Category: Structures of mtb proteins conferring susceptibility to known mtb inhibitor]] | ||
Revision as of 10:48, 9 December 2014
Crystal Structure of New Delhi Metal-beta-lactamase-1 from Klebsiella pneumoniae
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Categories: Beta-lactamase | Klebsiella pneumoniae | Babnigg, J | Binkowski, T A | Jedrzejczak, R | Joachimiak, A | Kim, Y | Structural genomic | MTBI, Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors | Mire, J | Sacchettini, J | Tesar, C | Alpha-beta structure | Hydrolase | Mcsg | Mtbi | Psi-biology | Structures of mtb proteins conferring susceptibility to known mtb inhibitor
