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1g68

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[[Image:1g68.jpg|left|200px]]
 
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{{Structure
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==PSE-4 CARBENICILLINASE, WILD TYPE==
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|PDB= 1g68 |SIZE=350|CAPTION= <scene name='initialview01'>1g68</scene>, resolution 1.95&Aring;
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<StructureSection load='1g68' size='340' side='right'caption='[[1g68]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1g68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G68 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]] 1.95&#8491;</td></tr>
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|GENE= PSE4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1g68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g68 OCA], [https://pdbe.org/1g68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g68 RCSB], [https://www.ebi.ac.uk/pdbsum/1g68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g68 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLP4_PSEAI BLP4_PSEAI] Hydrolyzes both carbenicillin and oxacillin.
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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/g6/1g68_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=1g68 ConSurf].
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<div style="clear:both"></div>
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'''PSE-4 CARBENICILLINASE, WILD TYPE'''
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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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PSE-4 is a class A beta-lactamase produced by strains of Pseudomonas aeruginosa and is highly active for the penicillin derivative carbenicillin. The crystal structure of the wild-type PSE-4 carbenicillinase has been determined to 1.95 A resolution by molecular replacement and represents the first structure of a carbenicillinase published to date. A superposition of the PSE-4 structure with that of TEM-1 shows a rms deviation of 1.3 A for 263 Calpha atoms. Most carbenicillinases are unique among class A beta-lactamases in that residue 234 is an arginine (ABL standard numbering scheme), while in all other class A enzymes this residue is a lysine. Kinetic characterization of a R234K PSE-4 mutant reveals a 50-fold reduction in k(cat)/K(m) and confirms the importance of Arg 234 for carbenicillinase activity. A comparison of the structure of the R234K mutant refined to 1.75 A resolution with the wild-type structure shows that Arg 234 stabilizes an alternate conformation of the Ser 130 side chain, not seen in other class A beta-lactamase structures. Our molecular modeling studies suggest that the position of a bound carbenicillin would be shifted relative to that of a bound benzylpenicillin in order to avoid a steric clash between the carbenicillin alpha-carboxylate group and the conserved side chain of Asn 170. The alternate conformation of the catalytic Ser 130 in wild-type PSE-4 may be involved in accommodating this shift in the bound substrate position.
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[[Category: Large Structures]]
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==About this Structure==
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1G68 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G68 OCA].
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==Reference==
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Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies., Lim D, Sanschagrin F, Passmore L, De Castro L, Levesque RC, Strynadka NC, Biochemistry. 2001 Jan 16;40(2):395-402. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11148033 11148033]
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[[Category: Beta-lactamase]]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: De Castro L]]
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[[Category: Castro, L De.]]
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[[Category: Levesque RC]]
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[[Category: Levesque, R C.]]
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[[Category: Lim D]]
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[[Category: Lim, D.]]
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[[Category: Passmore L]]
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[[Category: Passmore, L.]]
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[[Category: Sanschagrin F]]
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[[Category: Sanschagrin, F.]]
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[[Category: Strynadka NCJ]]
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[[Category: Strynadka, N C.J.]]
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[[Category: SO4]]
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[[Category: carbenicillinase]]
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[[Category: class a beta-lactamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:46 2008''
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Current revision

PSE-4 CARBENICILLINASE, WILD TYPE

PDB ID 1g68

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