|
|
| (12 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| [[Image:1fr1.gif|left|200px]]
| |
|
| |
|
| {{Structure
| | ==REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS== |
| |PDB= 1fr1 |SIZE=350|CAPTION= <scene name='initialview01'>1fr1</scene>, resolution 2.0Å
| | <StructureSection load='1fr1' size='340' side='right'caption='[[1fr1]], [[Resolution|resolution]] 2.00Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <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> |
| |ACTIVITY= <span class='plainlinks'>[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] </span>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| |GENE=
| | <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> |
| |DOMAIN= | | </table> |
| |RELATEDENTRY=[[1fr6|1FR6]]
| | == Function == |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr1 OCA], [http://www.ebi.ac.uk/pdbsum/1fr1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fr1 RCSB]</span>
| | [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/1fr1_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1fr1 ConSurf]. |
| | <div style="clear:both"></div> |
|
| |
|
| '''REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS'''
| | ==See Also== |
| | | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| 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==
| |
| 1FR1 is a [[Single protein]] structure of sequence from [http://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].
| |
| | |
| ==Reference==
| |
| 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://www.ncbi.nlm.nih.gov/pubmed/2300174 2300174]
| |
| [[Category: Beta-lactamase]]
| |
| [[Category: Citrobacter freundii]] | | [[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: antibiotic resistance]]
| |
| [[Category: class c beta-lactamase]]
| |
| [[Category: hydrolase]]
| |
| | |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:32 2008''
| |
