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==Crystal structure of ADC-1 beta-lactamase==
==Crystal structure of ADC-1 beta-lactamase==
<StructureSection load='4net' size='340' side='right' caption='[[4net]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='4net' size='340' side='right'caption='[[4net]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4net]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NET FirstGlance]. <br>
<table><tr><td colspan='2'>[[4net]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NET FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4net FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4net OCA], [https://pdbe.org/4net PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4net RCSB], [https://www.ebi.ac.uk/pdbsum/4net PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4net ProSAT]</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=4net FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4net OCA], [http://pdbe.org/4net PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4net RCSB], [http://www.ebi.ac.uk/pdbsum/4net PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4net ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q9L4R5_ACIBA Q9L4R5_ACIBA]
ADC-type class C beta-lactamases comprise a large group of enzymes that are encoded by genes located on the chromosome of Acinetobacter baumannii, a causative agent of serious bacterial infections. Overexpression of these enzymes renders A. baumannii resistant to various beta-lactam antibiotics and thus severely compromises the ability to treat infections caused by this deadly pathogen. Here, the high-resolution crystal structure of ADC-1, the first member of this clinically important family of antibiotic-resistant enzymes, is reported. Unlike the narrow-spectrum class C beta-lactamases, ADC-1 is capable of producing resistance to the expanded-spectrum cephalosporins, rendering them inactive against A. baumannii. The extension of the substrate profile of the enzyme is likely to be the result of structural differences in the R2-loop, primarily the deletion of three residues and subsequent rearrangement of the A10a and A10b helices. These structural rearrangements result in the enlargement of the R2 pocket of ADC-1, allowing it to accommodate the bulky R2 substituents of the third-generation cephalosporins, thus enhancing the catalytic efficiency of the enzyme against these clinically important antibiotics.
 
Structure of the extended-spectrum class C beta-lactamase ADC-1 from Acinetobacter baumannii.,Bhattacharya M, Toth M, Antunes NT, Smith CA, Vakulenko SB Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):760-71. doi:, 10.1107/S1399004713033014. Epub 2014 Feb 22. PMID:24598745<ref>PMID:24598745</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4net" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aciba]]
[[Category: Acinetobacter baumannii]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Antunes, N T]]
[[Category: Antunes NT]]
[[Category: Bhattacharya, M]]
[[Category: Bhattacharya M]]
[[Category: Smith, C A]]
[[Category: Smith CA]]
[[Category: Toth, M]]
[[Category: Toth M]]
[[Category: Vakulenko, S B]]
[[Category: Vakulenko SB]]
[[Category: Antibiotic resistance]]
[[Category: Apo enzyme]]
[[Category: Hydrolase]]
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