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1ceg

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[[Image:1ceg.gif|left|200px]]
 
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{{Structure
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==CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE==
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|PDB= 1ceg |SIZE=350|CAPTION= <scene name='initialview01'>1ceg</scene>, resolution 1.80&Aring;
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<StructureSection load='1ceg' size='340' side='right'caption='[[1ceg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACT:Those+For+S.+R61+Are+Listed+Below'>ACT</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CEP:CEPHALOTHIN GROUP'>CEP</scene>
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<table><tr><td colspan='2'>[[1ceg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._R61 Streptomyces sp. R61]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEG FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]
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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]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CEP:CEPHALOTHIN+GROUP'>CEP</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=1ceg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ceg OCA], [https://pdbe.org/1ceg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ceg RCSB], [https://www.ebi.ac.uk/pdbsum/1ceg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ceg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DAC_STRSR DAC_STRSR] Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).
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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/ce/1ceg_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=1ceg ConSurf].
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<div style="clear:both"></div>
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'''CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE'''
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==See Also==
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Two clinically-important beta-lactam antibiotics, cephalothin and cefotaxime, have been observed by X-ray crystallography bound to the reactive Ser62 of the D-alanyl-D-alanine carboxypeptidase/transpeptidase of Streptomyces sp. R61. Refinement of the two crystal structures produced R factors for 3 sigma (F) data of 0.166 (to 1.8 A) and 0.170 (to 2.0 A) for the cephalothin and cefotaxime complexes, respectively. In each complex, a water molecule is within 3.1 and 3.6 A of the acylated beta-lactam carbonyl carbon atom, but is poorly activated by active site residues for nucleophilic attack and deacylation. This apparent lack of good stereochemistry for facile hydrolysis is in accord with the long half-lives of cephalosporin intermediates in solution (20-40 h) and the efficacy of these beta-lactams as inhibitors of bacterial cell wall synthesis. Different hydrogen binding patterns of the two cephalosporins to Thr301 are consistent with the low cefotaxime affinity of an altered penicillin-binding protein, PBP-2x, reported in cefotaxime-resistant strains of Streptococcus pneumoniae, and with the ability of mutant class A beta-lactamases to hydrolyze third-generation cephalosporins.
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[[Category: Large Structures]]
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[[Category: Streptomyces sp. R61]]
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==About this Structure==
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[[Category: Knox JR]]
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1CEG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEG OCA].
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[[Category: Kuzin AP]]
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==Reference==
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Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7626623 7626623]
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[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
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[[Category: Single protein]]
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[[Category: Streptomyces sp.]]
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[[Category: Knox, J R.]]
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[[Category: Kuzin, A P.]]
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[[Category: CEP]]
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[[Category: d-amino acid peptidase]]
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[[Category: hydrolase-transpeptidase]]
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[[Category: penicillin target]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:19 2008''
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Current revision

CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE

PDB ID 1ceg

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