4oon: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4oon]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OON FirstGlance]. <br>
<table><tr><td colspan='2'>[[4oon]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OON FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2U4:(4Z,8S,11E,14S)-5-(2-AMINO-1,3-THIAZOL-4-YL)-14-(5,6-DIHYDROXY-1,3-DIOXO-1,3-DIHYDRO-2H-ISOINDOL-2-YL)-8-FORMYL-2-METHYL-6-OXO-3,10-DIOXA-4,7,11-TRIAZATETRADECA-4,11-DIENE-2,12,14-TRICARBOXYLIC+ACID'>2U4</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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2U4:(4Z,8S,11E,14S)-5-(2-AMINO-1,3-THIAZOL-4-YL)-14-(5,6-DIHYDROXY-1,3-DIOXO-1,3-DIHYDRO-2H-ISOINDOL-2-YL)-8-FORMYL-2-METHYL-6-OXO-3,10-DIOXA-4,7,11-TRIAZATETRADECA-4,11-DIENE-2,12,14-TRICARBOXYLIC+ACID'>2U4</scene></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=4oon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oon OCA], [https://pdbe.org/4oon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oon RCSB], [https://www.ebi.ac.uk/pdbsum/4oon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oon 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=4oon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oon OCA], [https://pdbe.org/4oon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oon RCSB], [https://www.ebi.ac.uk/pdbsum/4oon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oon ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PBPA_PSEAE PBPA_PSEAE] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (By similarity).
[https://www.uniprot.org/uniprot/PBPA_PSEAE PBPA_PSEAE] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multidrug-resistant Gram-negative pathogens are an emerging threat to human health, and addressing this challenge will require development of new antibacterial agents. This can be achieved through an improved molecular understanding of drug-target interactions combined with enhanced delivery of these agents to the site of action. Herein we describe the first application of siderophore receptor-mediated drug uptake of lactivicin analogues as a strategy that enables the development of novel antibacterial agents against clinically relevant Gram-negative bacteria. We report the first crystal structures of several sideromimic conjugated compounds bound to penicillin binding proteins PBP3 and PBP1a from Pseudomonas aeruginosa and characterize the reactivity of lactivicin and beta-lactam core structures. Results from drug sensitivity studies with beta-lactamase enzymes are presented, as well as a structure-based hypothesis to reduce susceptibility to this enzyme class. Finally, mechanistic studies demonstrating that sideromimic modification alters the drug uptake process are discussed.
Siderophore Receptor-Mediated Uptake of Lactivicin Analogues in Gram-Negative Bacteria.,Starr J, Brown MF, Aschenbrenner L, Caspers N, Che Y, Gerstenberger BS, Huband M, Knafels JD, Lemmon MM, Li C, McCurdy SP, McElroy E, Rauckhorst MR, Tomaras AP, Young JA, Zaniewski RP, Shanmugasundaram V, Han S J Med Chem. 2014 Apr 21. PMID:24694215<ref>PMID:24694215</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4oon" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>
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