1djb

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(New page: 200px<br /><applet load="1djb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1djb, resolution 2.1&Aring;" /> '''STRUCTURE OF BETA-LAC...)
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[[Image:1djb.jpg|left|200px]]<br /><applet load="1djb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1djb, resolution 2.1&Aring;" />
 
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'''STRUCTURE OF BETA-LACTAMASE PRECURSOR, S70A MUTANT, AT 298K'''<br />
 
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==Overview==
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==STRUCTURE OF BETA-LACTAMASE PRECURSOR, S70A MUTANT, AT 298K==
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Two mutant beta-lactamases from Staphylococcus aureus PC1 which probe key, catalytic residues have been produced by site-directed mutagenesis. In the, S70A enzyme, the nucleophilic group that attacks the beta-lactam carbonyl, carbon atom was eliminated. Consequently, the kcat values for hydrolysis, of benzylpenicillin and nitrocefin have been reduced by 10(4)-10(5), compared with the wild-type enzyme. The crystal structure of S70A, beta-lactamase has been determined at 2.1 A resolution. With the exception, of the mutation site, the structure is identical to that of the native, enzyme. The residual activity is attributed either to mistranslation that, leads to production of wild-type enzyme and/or to remaining features of, the active site that stabilize the tetrahedral transition state. Soaking, of the crystals with ampicillin or clavulanate, followed by, flash-freezing, has been carried out and the structures examined at 2.0 A, resolution. For both experiments, the difference electron density maps, revealed buildup of density in the active site that presumably corresponds, to beta-lactam binding. However, neither electron density is sufficiently, clear for defining the atomic details of the bound compounds. The K73H, beta-lactamase has been prepared to test the possible role of Lys73 in, proton transfer. It exhibits no detectable activity toward, benzylpenicillin, and 10(5)-fold reduction of kcat for nitrocefin, hydrolysis compared with the wild-type enzyme. No significant recovery of, activity has been measured when the pH was varied between 5.0 and 8.0. The, crystal structure of K73H beta-lactamase has been determined at 1.9 A, resolution. While the overall structure is similar to that of the native, enzyme, the electrostatic interactions between His73 and neighboring, residues indicate that the imidazole ring is positively charged. In, addition, the hydroxyl group of Ser70 adopts a position that is, incompatible with nucleophilic attack on substrates. A crystal soaked with, ampicillin was flash-frozen, and diffraction data were collected at 2.1 A, resolution. The electron density map showed no indication of substrate, binding.
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<StructureSection load='1djb' size='340' side='right'caption='[[1djb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1djb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJB 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]] 2.1&#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=1djb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1djb OCA], [https://pdbe.org/1djb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1djb RCSB], [https://www.ebi.ac.uk/pdbsum/1djb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1djb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLAC_STAAU BLAC_STAAU]
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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/dj/1djb_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=1djb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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=1DJB OCA].
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure and kinetics of the beta-lactamase mutants S70A and K73H from Staphylococcus aureus PC1., Chen CC, Smith TJ, Kapadia G, Wasch S, Zawadzke LE, Coulson A, Herzberg O, Biochemistry. 1996 Sep 24;35(38):12251-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8823158 8823158]
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[[Category: Large Structures]]
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[[Category: Beta-lactamase]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Chen, C.C.H.]]
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[[Category: Chen CCH]]
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[[Category: Herzberg, O.]]
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[[Category: Herzberg O]]
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[[Category: antibiotic resistance]]
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[[Category: hydrolase]]
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[[Category: plasmid]]
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[[Category: signal]]
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[[Category: transposable element]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:19:42 2007''
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STRUCTURE OF BETA-LACTAMASE PRECURSOR, S70A MUTANT, AT 298K

PDB ID 1djb

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