View source for 8rlk


==Structure of the apo form of PIB-1 in an Orthorombic space group==
<StructureSection load='8rlk' size='340' side='right'caption='[[8rlk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rlk]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RLK 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]] 2&#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=8rlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rlk OCA], [https://pdbe.org/8rlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rlk RCSB], [https://www.ebi.ac.uk/pdbsum/8rlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rlk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1J0J3U4_PSEAI A0A1J0J3U4_PSEAI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibiotic resistance is one of most important health concerns nowadays, and beta-lactamases are the most important resistance determinants. These enzymes, based on their structural and functional characteristics, are grouped in four categories (A, B, C and D). We have solved the structure of PIB-1, a Pseudomonas aeruginosa chromosomally-encoded beta-lactamase, in its apo form and in complex with meropenem and zinc. These crystal structures show that it belongs to the Class C beta-lactamase group, although it shows notable differences, especially in the Omega- and P2-loops, which are important for the enzymatic activity. Functional analysis showed that PIB-1 is able to degrade carbapenems but not cephalosporins, the typical substrate of Class C beta-lactamases, and that its catalytic activity increases in the presence of metal ions, especially zinc. They do not bind to the active-site but they induce the formation of trimers that show an increased capacity for the degradation of the antibiotics, suggesting that this oligomer is more active than the other oligomeric species. While PIB-1 is structurally a Class C beta-lactamase, the low sequence conservation, substrate profile and its metal-dependence, prompts us to position this enzyme as the founder of a new group inside the Class C beta-lactamases. Consequently, its diversity might be wider than expected.

A new type of Class C beta-lactamases defined by PIB-1. A metal-dependent carbapenem-hydrolyzing beta-lactamase, from Pseudomonas aeruginosa: Structural and functional analysis.,Medrano FJ, Hernando-Amado S, Martinez JL, Romero A Int J Biol Macromol. 2024 Aug 1:134298. doi: 10.1016/j.ijbiomac.2024.134298. PMID:39097051<ref>PMID:39097051</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rlk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Medrano FJ]]
[[Category: Romero A]]