View source for 5glc


==Crystal structure of the class A beta-lactamase PenL-tTR11 containing 20 residues insertion in omega-loop==
<StructureSection load='5glc' size='340' side='right'caption='[[5glc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5glc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_thailandensis Burkholderia thailandensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GLC 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]] 1.601&#8491;</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=5glc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glc OCA], [https://pdbe.org/5glc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5glc RCSB], [https://www.ebi.ac.uk/pdbsum/5glc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5glc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2T5A3_BURTA Q2T5A3_BURTA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The omega loop in beta-lactamases plays a pivotal role in substrate recognition and catalysis, and some mutations in this loop affect the adaptability of the enzymes to new antibiotics. Various mutations, including substitutions, deletions, and intragenic duplications resulting in tandem repeats (TRs), have been associated with beta-lactamase substrate spectrum extension. TRs are unique among the mutations as they cause severe structural perturbations in the enzymes. We explored the process by which TRs are accommodated in order to test the adaptability of the omega loop. Structures of the mutant enzymes showed that the extra amino acid residues in the omega loop were freed outward from the enzyme, thereby maintaining the overall enzyme integrity. This structural adjustment was accompanied by disruptions of the internal alpha-helix and hydrogen bonds that originally maintained the conformation of the omega loop and the active site. Consequently, the mutant enzymes had a relaxed binding cavity, allowing for access of new substrates, which regrouped upon substrate binding in an induced-fit manner for subsequent hydrolytic reactions. Together, the data demonstrate that the design of the binding cavity, including the omega loop with its enormous adaptive capacity, is the foundation of the continuous evolution of beta-lactamases against new drugs.

High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A beta-lactamase, PenL.,Yi H, Choi JM, Hwang J, Prati F, Cao TP, Lee SH, Kim HS Sci Rep. 2016 Nov 9;6:36527. doi: 10.1038/srep36527. PMID:27827433<ref>PMID:27827433</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5glc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia thailandensis]]
[[Category: Large Structures]]
[[Category: Choi JM]]
[[Category: Kim HS]]
[[Category: Lee SH]]
[[Category: Yi H]]