3n4i: Difference between revisions
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<StructureSection load='3n4i' size='340' side='right'caption='[[3n4i]], [[Resolution|resolution]] 1.56Å' scene=''> | <StructureSection load='3n4i' size='340' side='right'caption='[[3n4i]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3n4i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3n4i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] and [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N4I FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</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=3n4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n4i OCA], [https://pdbe.org/3n4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n4i RCSB], [https://www.ebi.ac.uk/pdbsum/3n4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n4i 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=3n4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n4i OCA], [https://pdbe.org/3n4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n4i RCSB], [https://www.ebi.ac.uk/pdbsum/3n4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n4i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BLA1_KLEPN BLA1_KLEPN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bonomo | [[Category: Streptomyces clavuligerus]] | ||
[[Category: Ghosh | [[Category: Bonomo RA]] | ||
[[Category: Handel | [[Category: Ghosh P]] | ||
[[Category: Hanes | [[Category: Handel TM]] | ||
[[Category: Kirsch | [[Category: Hanes MS]] | ||
[[Category: McNamara | [[Category: Kirsch JF]] | ||
[[Category: Reynolds | [[Category: McNamara C]] | ||
[[Category: Reynolds KA]] | |||
Latest revision as of 12:08, 6 September 2023
Crystal structure of the SHV-1 D104E beta-lactamase/beta-lactamase inhibitor protein (BLIP) complexCrystal structure of the SHV-1 D104E beta-lactamase/beta-lactamase inhibitor protein (BLIP) complex
Structural highlights
FunctionPublication Abstract from PubMedEstablishing a quantitative understanding of the determinants of affinity in protein-protein interactions remains challenging. For example, TEM-1/beta-lactamase inhibitor protein (BLIP) and SHV-1/BLIP are homologous beta-lactamase/beta-lactamase inhibitor protein complexes with disparate K(d) values (3 nM and 2 muM, respectively), and a single substitution, D104E in SHV-1, results in a 1000-fold enhancement in binding affinity. In TEM-1, E104 participates in a salt bridge with BLIP K74, whereas the corresponding SHV-1 D104 does not in the wild type SHV-1/BLIP co-structure. Here, we present a 1.6 A crystal structure of the SHV-1 D104E/BLIP complex that demonstrates that this point mutation restores this salt bridge. Additionally, mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400-fold increase in binding affinity. To understand how this salt bridge contributes to complex affinity, the cooperativity between the E/K or D/K salt bridge pair and a neighboring hot spot residue (BLIP F142) was investigated using double mutant cycle analyses in the background of the E73M mutation. We find that BLIP F142 cooperatively stabilizes both interactions, illustrating how a single mutation at a hot spot position can drive large perturbations in interface stability and specificity through a cooperative interaction network. Proteins 2011. (c) 2011 Wiley-Liss, Inc. Specificity and cooperativity at beta-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions.,Hanes MS, Reynolds KA, McNamara C, Ghosh P, Bonomo RA, Kirsch JF, Handel TM Proteins. 2010 Dec 13. doi: 10.1002/prot.22961. PMID:21294157[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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