View source for 8da2


==Acinetobacter baumannii L,D-transpeptidase==
<StructureSection load='8da2' size='340' side='right'caption='[[8da2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8da2]] is a 1 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=8DA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DA2 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]] 2.6&#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=8da2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8da2 OCA], [https://pdbe.org/8da2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8da2 RCSB], [https://www.ebi.ac.uk/pdbsum/8da2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8da2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A222A2P4_ACIBA A0A222A2P4_ACIBA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
l,d-Transpeptidases (LDTs) are enzymes that catalyze reactions essential for biogenesis of the bacterial cell wall, including formation of 3-3 cross-linked peptidoglycan. Unlike the historically well-known bacterial transpeptidases, the penicillin-binding proteins (PBPs), LDTs are resistant to inhibition by the majority of beta-lactam antibiotics, with the exception of carbapenems and penems, allowing bacteria to survive in the presence of these drugs. Here we report characterization of Ldt(Ab) from the clinically important pathogen, Acinetobacter baumannii. We show that A. baumannii survives inactivation of Ldt(Ab) alone or in combination with PBP1b or PBP2, while simultaneous inactivation of Ldt(Ab) and PBP1a is lethal. Minimal inhibitory concentrations (MICs) of all 13 beta-lactam antibiotics tested decreased 2- to 8-fold for the Ldt(Ab) deletion mutant, while further decreases were seen for both double mutants, with the largest, synergistic effect observed for the Ldt(Ab) + PBP2 deletion mutant. Mass spectrometry experiments showed that Ldt(Ab) forms complexes in vitro only with carbapenems. However, the acylation rate of these antibiotics is very slow, with the reaction taking longer than four hours to complete. Our X-ray crystallographic studies revealed that Ldt(Ab) has a unique structural architecture and is the only known LDT to have two different peptidoglycan-binding domains.

The l,d-Transpeptidase Ldt(Ab) from Acinetobacter baumannii Is Poorly Inhibited by Carbapenems and Has a Unique Structural Architecture.,Toth M, Stewart NK, Smith CA, Lee M, Vakulenko SB ACS Infect Dis. 2022 Sep 9;8(9):1948-1961. doi: 10.1021/acsinfecdis.2c00321. Epub , 2022 Aug 16. PMID:35973205<ref>PMID:35973205</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8da2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Smith CA]]
[[Category: Stewart NK]]
[[Category: Toth M]]
[[Category: Vakulenko SB]]