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1fr1

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(New page: 200px<br /><applet load="1fr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fr1, resolution 2.0&Aring;" /> '''REFINED CRYSTAL STRUC...)
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[[Image:1fr1.gif|left|200px]]<br /><applet load="1fr1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fr1, resolution 2.0&Aring;" />
 
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'''REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS'''<br />
 
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==Overview==
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==REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS==
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Beta-Lactamases (EC 3.5.2.6, 'penicillinases') are a family of enzymes, that protect bacteria against the lethal effects of cell-wall synthesis of, penicillins, cephalosporins and related antibiotic agents, by hydrolysing, the beta-lactam antibiotics to biologically inactive compounds. Their, production can, therefore, greatly contribute to the clinical problem of, antibiotic resistance. Three classes of beta-lactamases--A, B and C--have, been identified on the basis of their amino-acid sequence; class B, beta-lactamases are metalloenzymes, and are clearly distinct from members, of class A and C beta-lactamases, which both contain an active-site serine, residue involved in the formation of an acyl enzyme with beta-lactam, substrates during catalysis. It has been predicted that class C, beta-lactamases share common structural features with, D,D-carboxypeptidases and class A beta-lactamases, and further, suggested, that class A and class C beta-lactamases have the same evolutionary origin, as other beta-lactam target enzymes. We report here the refined, three-dimensional structure of the class C beta-lactamase from Citrobacter, freundii at 2.0-A resolution and confirm the predicted structural, similarity. The refined structure of the acyl-enzyme formed with the, monobactam inhibitor aztreonam at 2.5-A resolution defines the enzyme's, active site and, along with molecular modelling, indicates a mechanism for, beta-lactam hydrolysis. This leads to the hypothesis that Tyr 150, functions as a general base during catalysis.
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<StructureSection load='1fr1' size='340' side='right'caption='[[1fr1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FR1 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&#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=1fr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr1 OCA], [https://pdbe.org/1fr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fr1 RCSB], [https://www.ebi.ac.uk/pdbsum/1fr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fr1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q46041_CITFR Q46041_CITFR]
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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/fr/1fr1_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=1fr1 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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1FR1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. 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=1FR1 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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Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis., Oefner C, D'Arcy A, Daly JJ, Gubernator K, Charnas RL, Heinze I, Hubschwerlen C, Winkler FK, Nature. 1990 Jan 18;343(6255):284-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2300174 2300174]
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[[Category: Beta-lactamase]]
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[[Category: Citrobacter freundii]]
[[Category: Citrobacter freundii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arcy, A.D.]]
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[[Category: D'Arcy A]]
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[[Category: Daly, J.J.]]
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[[Category: Daly JJ]]
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[[Category: Oefner, C.]]
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[[Category: Oefner C]]
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[[Category: Winkler, F.K.]]
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[[Category: Winkler FK]]
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[[Category: antibiotic resistance]]
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[[Category: class c beta-lactamase]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:14:47 2007''
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Current revision

REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS

PDB ID 1fr1

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