1blp

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(New page: 200px<br /><applet load="1blp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1blp, resolution 2.3&Aring;" /> '''STRUCTURAL BASIS FOR ...)
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[[Image:1blp.gif|left|200px]]<br /><applet load="1blp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1blp, resolution 2.3&Aring;" />
 
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'''STRUCTURAL BASIS FOR THE INACTIVATION OF THE P54 MUTANT OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1'''<br />
 
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==Overview==
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==STRUCTURAL BASIS FOR THE INACTIVATION OF THE P54 MUTANT OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1==
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The crystal structure of a mutant protein of a class A beta-lactamase from, Staphylococcus aureus PC1, in which Asp179 is replaced by an asparagine, (P54), has been determined and refined at 2.3-A resolution (1 A = 0.1 nm)., The resulting crystallographic R factor [formula: see text] are the, observed and calculated structure factor amplitudes) is 0.181 for 12289, reflections with I greater than or equal to sigma (I) within the 6.0-2.3-A, resolution range. The mutated residue is located at the C-terminus of an, extensive loop (the omega-loop), remote from the active site, and results, in a drastically reduced activity. Examination of the native and P54, structures reveals that the overall fold is similar, except that there is, substantial disorder of the omega-loop of P54. This is a consequence of, the elimination of a salt bridge between Asp179 and Arg164 that links the, two ends of the omega-loop in native beta-lactamase. It is associated with, a difference in side-chain conformation between Asn179 in P54 and Asp179, in the native structure. An alternate interaction occurs in P54 between, Asn179 and Ala69, adjacent to the catalytic Ser70. This disorder affects, catalysis since some of the disordered residues, in particular Glu166, form part of the active site.(ABSTRACT TRUNCATED AT 250 WORDS)
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<StructureSection load='1blp' size='340' side='right'caption='[[1blp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1blp]] 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=1BLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BLP 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]] 2.3&#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=1blp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1blp OCA], [https://pdbe.org/1blp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1blp RCSB], [https://www.ebi.ac.uk/pdbsum/1blp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1blp 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/bl/1blp_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=1blp 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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1BLP 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=1BLP 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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Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1., Herzberg O, Kapadia G, Blanco B, Smith TS, Coulson A, Biochemistry. 1991 Oct 1;30(39):9503-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1892849 1892849]
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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: Herzberg, O.]]
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[[Category: Herzberg O]]
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[[Category: hydrolase(acting on cyclic amides)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:44:47 2007''
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Current revision

STRUCTURAL BASIS FOR THE INACTIVATION OF THE P54 MUTANT OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1

PDB ID 1blp

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