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1kge

From Proteopedia

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[[Image:1kge.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT==
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|PDB= 1kge |SIZE=350|CAPTION= <scene name='initialview01'>1kge</scene>, resolution 2.0&Aring;
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<StructureSection load='1kge' size='340' side='right'caption='[[1kge]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1kge]] 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=1KGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KGE FirstGlance]. <br>
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|ACTIVITY= [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]
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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&#8491;</td></tr>
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|GENE= BLAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
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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=1kge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kge OCA], [https://pdbe.org/1kge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kge RCSB], [https://www.ebi.ac.uk/pdbsum/1kge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kge ProSAT]</span></td></tr>
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}}
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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/kg/1kge_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=1kge ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT'''
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Two site-directed mutant enzymes of the class A beta-lactamase from Staphylococcus aureus PC1 were produced with the goal of blocking the site that in the native enzyme is occupied by the proposed hydrolytic water molecule. The crystal structures of these two mutant enzymes, N170Q and N170M, have been determined and refined at 2.2 and 2.0 A, respectively. They reveal that the side chain of Gln 170 displaces the water molecule, whereas that of Met170 does not. In both cases, the catalytic rates with benzylpenicillin are reduced by 10(4) compared with the native enzyme. With nitrocefin, the N170Q mutant enzyme exhibits an approximately 800-fold reduced rate compared with the native enzyme and in addition, a fast initial burst with stoichiometry of 1 mol of degraded nitrocefin/mol of enzyme. Stopped-flow kinetic experiments establish that the rate constant of the burst is 250 s-1, a value comparable with the rate of acylation of the native enzyme. Two structurally based mechanisms that explain the kinetic properties of the N170Q beta-lactamase are proposed, both invoking a deacylation-impaired enzyme due to the elimination of the hydrolytic water molecule. The catalytic rate of the N170M mutant enzyme with nitrocefin is reduced by approximately 50-fold compared with the native enzyme, and the slow progressive inhibition that is revealed indicates that the hydrolysis proceeds via a branched pathway mechanism. This is consistent with the structural data that show that the water site is preserved and that Met170 occupies part of the space that is required for substrate binding. The short contacts between the substrate and the enzyme may lead to structure perturbation and inactivation.
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[[Category: Large Structures]]
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==About this Structure==
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1KGE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGE OCA].
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==Reference==
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Elimination of the hydrolytic water molecule in a class A beta-lactamase mutant: crystal structure and kinetics., Zawadzke LE, Chen CC, Banerjee S, Li Z, Wasch S, Kapadia G, Moult J, Herzberg O, Biochemistry. 1996 Dec 24;35(51):16475-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8987980 8987980]
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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: Zawadzke, L E.]]
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[[Category: Zawadzke LE]]
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[[Category: antibiotic resistance]]
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[[Category: beta-lactamase]]
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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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:17:08 2008''
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Current revision

STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT

PDB ID 1kge

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