1r77: Difference between revisions

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 <StructureSection load='1r77' size='340' side='right'caption='[[1r77]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1r77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27840 Atcc 27840]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R77 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1r77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_capitis Staphylococcus capitis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R77 FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r77 OCA], [http://pdbe.org/1r77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r77 RCSB], [http://www.ebi.ac.uk/pdbsum/1r77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r77 ProSAT]</span></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=1r77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r77 OCA], [https://pdbe.org/1r77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r77 RCSB], [https://www.ebi.ac.uk/pdbsum/1r77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r77 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ALE1_STACP ALE1_STACP]] Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan.
+[https://www.uniprot.org/uniprot/ALE1_STACP ALE1_STACP] Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1r77 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-ALE-1, a homologue of lysostaphin, is a peptidoglycan hydrolase that specifically lyses Staphylococcus aureus cell walls by cleaving the pentaglycine linkage between the peptidoglycan chains. Binding of ALE-1 to S. aureus cells through its C-terminal 92 residues, known as the targeting domain, is functionally important for staphylolytic activity. The ALE-1-targeting domain belongs to the SH3b domain family, the prokaryotic counterpart of the eukaryotic SH3 domains. The 1.75 angstroms crystal structure of the targeting domain shows an all-beta fold similar to typical SH3s but with unique features. The structure reveals patches of conserved residues among orthologous targeting domains, forming surface regions that can potentially interact with some common features of the Gram-positive cell wall. ALE-1-targeting domain binding studies employing various bacterial peptidoglycans demonstrate that the length of the interpeptide bridge, as well as the amino acid composition of the peptide, confers the maximum binding of the targeting domain to the staphylococcal peptidoglycan. Truncation of the highly conserved first 9 N-terminal residues results in loss of specificity to S. aureus cell wall-targeting, suggesting that these residues confer specificity to S. aureus cell wall.
-Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges.,Lu JZ, Fujiwara T, Komatsuzawa H, Sugai M, Sakon J J Biol Chem. 2006 Jan 6;281(1):549-58. Epub 2005 Oct 28. PMID:16257954<ref>PMID:16257954</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1r77" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 27840]]
-[[Category: Interstitial collagenase]]
 [[Category: Large Structures]]
-[[Category: Fujiwara, T]]
+[[Category: Staphylococcus capitis]]
-[[Category: Komatsuzawa, H]]
+[[Category: Fujiwara T]]
-[[Category: Lu, J Z]]
+[[Category: Komatsuzawa H]]
-[[Category: Sakon, J]]
+[[Category: Lu JZ]]
-[[Category: Sugai, M]]
+[[Category: Sakon J]]
-[[Category: Cell wall targeting domain]]
+[[Category: Sugai M]]
-[[Category: Glycylglycine endopeptidase]]
-[[Category: Hydrolase]]
-[[Category: Lysostaphin]]
-[[Category: Peptidoglycan hydrolase]]
-[[Category: Sh3b domain]]