3qi0

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Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein-II (BLIP-II) with class A beta-lactamases

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 <StructureSection load='3qi0' size='340' side='right'caption='[[3qi0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qi0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_exfoliatus"_waksman_and_curtis_1916 "actinomyces exfoliatus" waksman and curtis 1916]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QI0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qi0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_exfoliatus Streptomyces exfoliatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QI0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jtg|1jtg]], [[1jtd|1jtd]], [[3qhy|3qhy]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bliB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1905 "Actinomyces exfoliatus" Waksman and Curtis 1916])</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=3qi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qi0 OCA], [https://pdbe.org/3qi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qi0 RCSB], [https://www.ebi.ac.uk/pdbsum/3qi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qi0 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/O87916_STREX O87916_STREX]
-beta-Lactamases hydrolyze beta-lactam antibiotics to provide drug resistance to bacteria. beta-Lactamase inhibitory protein-II (BLIP-II) is a potent proteinaceous inhibitor that exhibits low picomolar affinity for class A beta-lactamases. This study examines the driving forces for binding between BLIP-II and beta-lactamases using a combination of presteady state kinetics, isothermal titration calorimetry, and x-ray crystallography. The measured dissociation rate constants for BLIP-II and various beta-lactamases ranged from 10(-4) to 10(-7) s(-1) and are comparable with those found in some of the tightest known protein-protein interactions. The crystal structures of BLIP-II alone and in complex with Bacillus anthracis Bla1 beta-lactamase revealed no significant side-chain movement in BLIP-II in the complex versus the monomer. The structural rigidity of BLIP-II minimizes the loss of the entropy upon complex formation and, as indicated by thermodynamics experiments, may be a key determinant of the observed potent inhibition of beta-lactamases.
-Analysis of the binding forces driving the tight interactions between beta-lactamase inhibitory protein-II (BLIP-II) and class A beta-lactamases.,Brown NG, Chow DC, Sankaran B, Zwart P, Prasad BV, Palzkill T J Biol Chem. 2011 Sep 16;286(37):32723-35. Epub 2011 Jul 20. PMID:21775426<ref>PMID:21775426</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3qi0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)|TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Actinomyces exfoliatus waksman and curtis 1916]]
 [[Category: Large Structures]]
-[[Category: Brown, N G]]
+[[Category: Streptomyces exfoliatus]]
-[[Category: Chow, D C]]
+[[Category: Brown NG]]
-[[Category: Palzkill, T]]
+[[Category: Chow DC]]
-[[Category: Prasad, B V.V]]
+[[Category: Palzkill T]]
-[[Category: Sankaran, B]]
+[[Category: Prasad BVV]]
-[[Category: Zwart, P]]
+[[Category: Sankaran B]]
-[[Category: Beta-lactamase]]
+[[Category: Zwart P]]
-[[Category: Beta-propeller]]
-[[Category: Bsgc]]
-[[Category: Enzyme-inhibitor complex]]
-[[Category: Hydrolase inhibitor]]
-[[Category: Protein:protein interaction]]

3qi0

From Proteopedia

Current revision

Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein-II (BLIP-II) with class A beta-lactamases

Structural highlights

Function

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