3oc2

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Current revision (10:04, 14 February 2024) (edit) (undo)
 
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<StructureSection load='3oc2' size='340' side='right'caption='[[3oc2]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='3oc2' size='340' side='right'caption='[[3oc2]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3oc2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OC2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3oc2]] is a 1 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=3OC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OC2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.968&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA4418 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=3oc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oc2 OCA], [https://pdbe.org/3oc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oc2 RCSB], [https://www.ebi.ac.uk/pdbsum/3oc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oc2 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=3oc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oc2 OCA], [https://pdbe.org/3oc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oc2 RCSB], [https://www.ebi.ac.uk/pdbsum/3oc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oc2 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q51504_PSEAI Q51504_PSEAI]
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We report the first crystal structures of a penicillin-binding protein (PBP), PBP3, from Pseudomonas aeruginosa in native form and covalently linked to two important beta-lactam antibiotics, carbenicillin and ceftazidime. Overall, the structures of apo and acyl complexes are very similar; however, variations in the orientation of the amino-terminal membrane-proximal domain relative to that of the carboxy-terminal transpeptidase domain indicate interdomain flexibility. Binding of either carbenicillin or ceftazidime to purified PBP3 increases the thermostability of the enzyme significantly and is associated with local conformational changes, which lead to a narrowing of the substrate-binding cleft. The orientations of the two beta-lactams in the active site and the key interactions formed between the ligands and PBP3 are similar despite differences in the two drugs, indicating a degree of flexibility in the binding site. The conserved binding mode of beta-lactam-based inhibitors appears to extend to other PBPs, as suggested by a comparison of the PBP3/ceftazidime complex and the Escherichia coli PBP1b/ceftoxamine complex. Since P. aeruginosa is an important human pathogen, the structural data reveal the mode of action of the frontline antibiotic ceftazidime at the molecular level. This study seeks improved drugs to combat infections by P. aeruginosa and related Gram-negative bacteria and also provides templates to assist that process and to allow us to discuss new ways of inhibiting PBPs.
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Crystal Structures of Penicillin-Binding Protein 3 from Pseudomonas aeruginosa: Comparison of Native and Antibiotic-Bound Forms.,Sainsbury S, Bird L, Rao V, Shepherd SM, Stuart DI, Hunter WN, Owens RJ, Ren J J Mol Biol. 2010 Oct 23. PMID:20974151<ref>PMID:20974151</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3oc2" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bird, L]]
 
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[[Category: OPPF, Oxford Protein Production Facility]]
 
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[[Category: Owens, R J]]
 
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[[Category: Ren, J]]
 
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[[Category: Sainsbury, S]]
 
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[[Category: Stuart, D I]]
 
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[[Category: Cell wall biosynthesis]]
 
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[[Category: Oppf]]
 
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[[Category: Out periplasmic membrane]]
 
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[[Category: Oxford protein production facility]]
 
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[[Category: Penicillin-binding protein]]
 
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Structural genomic]]
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[[Category: Bird L]]
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[[Category: Transpeptidase]]
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[[Category: Owens RJ]]
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[[Category: Ren J]]
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[[Category: Sainsbury S]]
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[[Category: Stuart DI]]

Current revision

Crystal structure of penicillin-binding protein 3 from Pseudomonas aeruginosa

PDB ID 3oc2

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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