3n8s: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Crystal Structure of BlaC-E166A covalently bound with Cefamandole== | ||
<StructureSection load='3n8s' size='340' side='right'caption='[[3n8s]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3n8s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N8S FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=XD2:(2R)-2-[(1R)-1-{[(2R)-2-HYDROXY-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5-{[(1-METHYL-1H-TETRAZOL-5-YL)SULFANYL]METHYL}-3,6-DIHYDRO-2H-1,3-THIAZINE-4-CARBOXYLIC+ACID'>XD2</scene></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=3n8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n8s OCA], [https://pdbe.org/3n8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n8s RCSB], [https://www.ebi.ac.uk/pdbsum/3n8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n8s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BLAC_MYCTU BLAC_MYCTU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The genome of Mycobacterium tuberculosis (TB) contains a gene that encodes a highly active beta-lactamase, BlaC, that imparts TB with resistance to beta-lactam chemotherapy. The structure of covalent BlaC-beta-lactam complexes suggests that active site residues K73 and E166 are essential for acylation and deacylation, respectively. We have prepared the K73A and E166A mutant forms of BlaC and have determined the structures of the Michaelis complex of cefamandole and the covalently bound acyl intermediate of cefamandole at resolutions of 1.2 and 2.0 A, respectively. These structures provide insight into the details of the catalytic mechanism. | |||
Structures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants .,Tremblay LW, Xu H, Blanchard JS Biochemistry. 2010 Nov 16;49(45):9685-7. Epub 2010 Oct 25. PMID:20961112<ref>PMID:20961112</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3n8s" style="background-color:#fffaf0;"></div> | |||
== | |||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Blanchard | [[Category: Blanchard JS]] | ||
[[Category: Tremblay | [[Category: Tremblay LW]] | ||
Latest revision as of 12:27, 30 October 2024
Crystal Structure of BlaC-E166A covalently bound with CefamandoleCrystal Structure of BlaC-E166A covalently bound with Cefamandole
Structural highlights
FunctionPublication Abstract from PubMedThe genome of Mycobacterium tuberculosis (TB) contains a gene that encodes a highly active beta-lactamase, BlaC, that imparts TB with resistance to beta-lactam chemotherapy. The structure of covalent BlaC-beta-lactam complexes suggests that active site residues K73 and E166 are essential for acylation and deacylation, respectively. We have prepared the K73A and E166A mutant forms of BlaC and have determined the structures of the Michaelis complex of cefamandole and the covalently bound acyl intermediate of cefamandole at resolutions of 1.2 and 2.0 A, respectively. These structures provide insight into the details of the catalytic mechanism. Structures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants .,Tremblay LW, Xu H, Blanchard JS Biochemistry. 2010 Nov 16;49(45):9685-7. Epub 2010 Oct 25. PMID:20961112[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||