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<StructureSection load='3ny4' size='340' side='right'caption='[[3ny4]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
<StructureSection load='3ny4' size='340' side='right'caption='[[3ny4]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ny4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NY4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ny4]] 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=3NY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NY4 FirstGlance]. <br>
</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=SMX:(6R,7R)-7-{[(2R)-2-HYDROXY-2-PHENYLACETYL]AMINO}-3-{[(1-METHYL-1H-TETRAZOL-5-YL)SULFANYL]METHYL}-8-OXO-5-THIA-1-AZABICYCLO[4.2.0]OCT-2-ENE-2-CARBOXYLIC+ACID'>SMX</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]] 1.22&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaA, blaC, Rv2068c, MT2128, MTCY49.07c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=SMX:(6R,7R)-7-{[(2R)-2-HYDROXY-2-PHENYLACETYL]AMINO}-3-{[(1-METHYL-1H-TETRAZOL-5-YL)SULFANYL]METHYL}-8-OXO-5-THIA-1-AZABICYCLO[4.2.0]OCT-2-ENE-2-CARBOXYLIC+ACID'>SMX</scene></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ny4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ny4 OCA], [https://pdbe.org/3ny4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ny4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ny4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ny4 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=3ny4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ny4 OCA], [https://pdbe.org/3ny4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ny4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ny4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ny4 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/BLAC_MYCTU BLAC_MYCTU]
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ny4" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blanchard, J S]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Tremblay, L W]]
[[Category: Blanchard JS]]
[[Category: Beta-lactam complex]]
[[Category: Tremblay LW]]
[[Category: Hydrolase-antibiotic complex]]
[[Category: Penicillin binding protein]]

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