1skf: Difference between revisions

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OCA

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-[[Image:1skf.gif|left|200px]]<br />
-<applet load="1skf" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1skf, resolution 2.00&Aring;" />
-'''CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE==
-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)]]
+<StructureSection load='1skf' size='340' side='right'caption='[[1skf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DACX_STRSK DACX_STRSK] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
+== 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/sk/1skf_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=1skf ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-SKF 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SKF OCA]].
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
+*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
-==Reference==
+__TOC__
-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]
+</StructureSection>
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Streptomyces sp.]]
+[[Category: Streptomyces sp. K15]]
-[[Category: Charlier, P.]]
+[[Category: Charlier P]]
-[[Category: Fonze, E.]]
+[[Category: Fonze E]]
-[[Category: beta-lactamase]]
-[[Category: dd-transpeptidase]]
-[[Category: hydrolase carboxypeptidase]]
-[[Category: penicillin-binding]]
-[[Category: serine peptidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:57:24 2007''