1fr6: Difference between revisions

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OCA

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-[[Image:1fr6.gif|left|200px]]<br /><applet load="1fr6" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fr6, resolution 2.5&Aring;" />
-'''REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS'''<br />
-==Overview==
+==REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS==
-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.
+<StructureSection load='1fr6' size='340' side='right'caption='[[1fr6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fr6]] 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=1FR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FR6 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZR:2-({[(1Z)-1-(2-AMINO-1,3-THIAZOL-4-YL)-2-OXO-2-{[(2S,3S)-1-OXO-3-(SULFOAMINO)BUTAN-2-YL]AMINO}ETHYLIDENE]AMINO}OXY)-2-METHYLPROPANOIC+ACID'>AZR</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr6 OCA], [https://pdbe.org/1fr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fr6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q46041_CITFR Q46041_CITFR]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1fr6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1fr6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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:2300174<ref>PMID:2300174</ref>
-FR6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii] with AZR as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FR6 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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]
+</div>
-[[Category: Beta-lactamase]]
+<div class="pdbe-citations 1fr6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Citrobacter freundii]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Arcy, A.D.]]
+[[Category: D'Arcy A]]
-[[Category: Daly, J.J.]]
+[[Category: Daly JJ]]
-[[Category: Oefner, C.]]
+[[Category: Oefner C]]
-[[Category: Winkler, F.K.]]
+[[Category: Winkler FK]]
-[[Category: AZR]]
-[[Category: antibiotic resistance]]
-[[Category: class c beta-lactamase]]
-[[Category: hydrolase]]
-[[Category: monobactum]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:15:34 2007''