|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of NDM-1 bound to hydrolyzed oxacillin== | | ==Crystal structure of NDM-1 bound to hydrolyzed oxacillin== |
| - | <StructureSection load='4eyb' size='340' side='right' caption='[[4eyb]], [[Resolution|resolution]] 1.16Å' scene=''> | + | <StructureSection load='4eyb' size='340' side='right'caption='[[4eyb]], [[Resolution|resolution]] 1.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4eyb]] is a 2 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=4EYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EYB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4eyb]] is a 2 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=4EYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EYB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0WO:(2R,4S)-2-[(R)-CARBOXY{[(5-METHYL-3-PHENYL-1,2-OXAZOL-4-YL)CARBONYL]AMINO}METHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>0WO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0WO:(2R,4S)-2-[(R)-CARBOXY{[(5-METHYL-3-PHENYL-1,2-OXAZOL-4-YL)CARBONYL]AMINO}METHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>0WO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q6x|3q6x]], [[3spu|3spu]], [[4exs|4exs]], [[4exy|4exy]], [[4ey2|4ey2]], [[4eyf|4eyf]], [[4eyl|4eyl]]</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=4eyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyb OCA], [https://pdbe.org/4eyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eyb RCSB], [https://www.ebi.ac.uk/pdbsum/4eyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eyb ProSAT]</span></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 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</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=4eyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyb OCA], [http://pdbe.org/4eyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eyb RCSB], [http://www.ebi.ac.uk/pdbsum/4eyb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eyb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 4eyb" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4eyb" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | + | [[Category: Klebsiella pneumoniae]] |
| - | [[Category: King, D T]] | + | [[Category: Large Structures]] |
| - | [[Category: Strynadka, N C.J]] | + | [[Category: King DT]] |
| - | [[Category: Antibiotic]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Hydrolase-antibiotic complex]]
| + | |
| - | [[Category: Metallo beta lactamase]]
| + | |
| Structural highlights
Function
BLAN1_KLEPN Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
Publication Abstract from PubMed
The beta-lactam antibiotics have long been a cornerstone for the treatment of bacterial disease. Recently, a readily transferable antibiotic resistance factor called the New Delhi metallo-beta-lactamase-1 (NDM-1) has been found to confer enteric bacteria resistance to nearly all beta-lactams, including the heralded carbapenems, posing a serious threat to human health. The crystal structure of NDM-1 bound to meropenem shows for the first time the molecular details of how carbapenem antibiotics are recognized by dizinc-containing metallo-beta-lactamases. Additionally, product complex structures of hydrolyzed benzylpenicillin-, methicillin-, and oxacillin-bound NDM-1 have been solved to 1.8, 1.2, and 1.2 A, respectively, and represent the highest-resolution structural data for any metallo-beta-lactamase reported to date. Finally, we present the crystal structure of NDM-1 bound to the potent competitive inhibitor l-captopril, which reveals a unique binding mechanism. An analysis of the NDM-1 active site in these structures reveals key features important for the informed design of novel inhibitors of NDM-1 and other metallo-beta-lactamases.
New Delhi Metallo-beta-Lactamase: Structural Insights into beta-Lactam Recognition and Inhibition.,King DT, Worrall LJ, Gruninger R, Strynadka NC J Am Chem Soc. 2012 Jul 18;134(28):11362-5. Epub 2012 Jul 5. PMID:22713171[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ King DT, Worrall LJ, Gruninger R, Strynadka NC. New Delhi Metallo-beta-Lactamase: Structural Insights into beta-Lactam Recognition and Inhibition. J Am Chem Soc. 2012 Jul 18;134(28):11362-5. Epub 2012 Jul 5. PMID:22713171 doi:10.1021/ja303579d
|
