1skf

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[[Image:1skf.gif|left|200px]]<br />
 
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<applet load="1skf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1skf, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE==
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The serine DD-transpeptidase/penicillin-binding protein of Streptomyces, K15 catalyzes peptide bond formation in a way that mimics the, penicillin-sensitive peptide cross-linking reaction involved in bacterial, cell wall peptidoglycan assembly. The Streptomyces K15 enzyme is peculiar, in that it can be considered as an intermediate between classical, penicillin-binding proteins, for which benzylpenicillin is a very, efficient inactivator, and the resistant penicillin-binding proteins that, have a low penicillin affinity. With its moderate penicillin sensitivity, the Streptomyces K15 DD-transpeptidase would be helpful in the, understanding of the structure-activity relationship of this, penicillin-recognizing protein superfamily. The structure of the, Streptomyces K15 enzyme has been ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10419503 (full description)]]
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<StructureSection load='1skf' size='340' side='right'caption='[[1skf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1skf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._K15 Streptomyces sp. K15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SKF 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=1skf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1skf OCA], [https://pdbe.org/1skf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1skf RCSB], [https://www.ebi.ac.uk/pdbsum/1skf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1skf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DACX_STRSK DACX_STRSK] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
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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/sk/1skf_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=1skf 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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1SKF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]]. Active as [[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]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SKF OCA]].
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
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==Reference==
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__TOC__
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The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15., Fonze E, Vermeire M, Nguyen-Disteche M, Brasseur R, Charlier P, J Biol Chem. 1999 Jul 30;274(31):21853-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10419503 10419503]
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</StructureSection>
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[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Streptomyces sp. K15]]
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[[Category: Streptomyces sp.]]
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[[Category: Charlier P]]
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[[Category: Charlier, P.]]
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[[Category: Fonze E]]
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[[Category: Fonze, E.]]
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[[Category: beta-lactamase]]
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[[Category: dd-transpeptidase]]
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[[Category: hydrolase carboxypeptidase]]
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[[Category: penicillin-binding]]
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[[Category: serine peptidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:53:37 2007''
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Current revision

CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE

PDB ID 1skf

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