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2g2w

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(New page: 200px<br /><applet load="2g2w" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g2w, resolution 1.80&Aring;" /> '''Crystal Structure of...)
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[[Image:2g2w.gif|left|200px]]<br /><applet load="2g2w" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2g2w, resolution 1.80&Aring;" />
 
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'''Crystal Structure of the SHV D104K Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) complex'''<br />
 
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==Overview==
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==Crystal Structure of the SHV D104K Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) complex==
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Beta-lactamase inhibitor protein (BLIP) binds a variety of class A, beta-lactamases with affinities ranging from micromolar to picomolar., Whereas the TEM-1 and SHV-1 beta-lactamases are almost structurally, identical, BLIP binds TEM-1 approximately 1000-fold tighter than SHV-1., Determining the underlying source of this affinity difference is important, for understanding the molecular basis of beta-lactamase inhibition and, mechanisms of protein-protein interface specificity and affinity. Here we, present the 1.6A resolution crystal structure of SHV-1.BLIP. In addition, a point mutation was identified, SHV D104E, that increases SHV.BLIP, binding affinity from micromolar to nanomolar. Comparison of the, SHV-1.BLIP structure with the published TEM-1.BLIP structure suggests that, the increased volume of Glu-104 stabilizes a key binding loop in the, interface. Solution of the 1.8A SHV D104K.BLIP crystal structure, identifies a novel conformation in which this binding loop is removed from, the interface. Using these structural data, we evaluated the ability of, EGAD, a program developed for computational protein design, to calculate, changes in the stability of mutant beta-lactamase.BLIP complexes. Changes, in binding affinity were calculated within an error of 1.6 kcal/mol of the, experimental values for 112 mutations at the TEM-1.BLIP interface and, within an error of 2.2 kcal/mol for 24 mutations at the SHV-1.BLIP, interface. The reasonable success of EGAD in predicting changes in, interface stability is a promising step toward understanding the stability, of the beta-lactamase.BLIP complexes and computationally assisted design, of tight binding BLIP variants.
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<StructureSection load='2g2w' size='340' side='right'caption='[[2g2w]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2g2w]] 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=2G2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G2W FirstGlance]. <br>
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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]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g2w OCA], [https://pdbe.org/2g2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g2w RCSB], [https://www.ebi.ac.uk/pdbsum/2g2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g2w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLA1_KLEPN BLA1_KLEPN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/2g2w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g2w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Beta-lactamase inhibitor protein (BLIP) binds a variety of class A beta-lactamases with affinities ranging from micromolar to picomolar. Whereas the TEM-1 and SHV-1 beta-lactamases are almost structurally identical, BLIP binds TEM-1 approximately 1000-fold tighter than SHV-1. Determining the underlying source of this affinity difference is important for understanding the molecular basis of beta-lactamase inhibition and mechanisms of protein-protein interface specificity and affinity. Here we present the 1.6A resolution crystal structure of SHV-1.BLIP. In addition, a point mutation was identified, SHV D104E, that increases SHV.BLIP binding affinity from micromolar to nanomolar. Comparison of the SHV-1.BLIP structure with the published TEM-1.BLIP structure suggests that the increased volume of Glu-104 stabilizes a key binding loop in the interface. Solution of the 1.8A SHV D104K.BLIP crystal structure identifies a novel conformation in which this binding loop is removed from the interface. Using these structural data, we evaluated the ability of EGAD, a program developed for computational protein design, to calculate changes in the stability of mutant beta-lactamase.BLIP complexes. Changes in binding affinity were calculated within an error of 1.6 kcal/mol of the experimental values for 112 mutations at the TEM-1.BLIP interface and within an error of 2.2 kcal/mol for 24 mutations at the SHV-1.BLIP interface. The reasonable success of EGAD in predicting changes in interface stability is a promising step toward understanding the stability of the beta-lactamase.BLIP complexes and computationally assisted design of tight binding BLIP variants.
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==About this Structure==
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Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface.,Reynolds KA, Thomson JM, Corbett KD, Bethel CR, Berger JM, Kirsch JF, Bonomo RA, Handel TM J Biol Chem. 2006 Sep 8;281(36):26745-53. Epub 2006 Jun 29. PMID:16809340<ref>PMID:16809340</ref>
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2G2W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] and [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G2W OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface., Reynolds KA, Thomson JM, Corbett KD, Bethel CR, Berger JM, Kirsch JF, Bonomo RA, Handel TM, J Biol Chem. 2006 Sep 8;281(36):26745-53. Epub 2006 Jun 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16809340 16809340]
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</div>
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[[Category: Beta-lactamase]]
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<div class="pdbe-citations 2g2w" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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*[[TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)|TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Klebsiella pneumoniae]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Streptomyces clavuligerus]]
[[Category: Streptomyces clavuligerus]]
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[[Category: Berger, J.M.]]
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[[Category: Berger JM]]
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[[Category: Bethel, C.R.]]
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[[Category: Bethel CR]]
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[[Category: Bonomo, R.A.]]
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[[Category: Bonomo RA]]
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[[Category: Corbett, K.D.]]
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[[Category: Corbett KD]]
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[[Category: Handel, T.M.]]
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[[Category: Handel TM]]
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[[Category: Kirsch, J.F.]]
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[[Category: Kirsch JF]]
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[[Category: Reynolds, K.A.]]
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[[Category: Reynolds KA]]
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[[Category: Thomson, J.M.]]
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[[Category: Thomson JM]]
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[[Category: beta-lactamase]]
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[[Category: beta-lactamase inhibitor]]
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[[Category: blip]]
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[[Category: protein-protein complex]]
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[[Category: shv]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:55:16 2007''
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Current revision

Crystal Structure of the SHV D104K Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) complex

PDB ID 2g2w

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