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5wqw

From Proteopedia

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Current revision (09:18, 20 March 2024) (edit) (undo)
 
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<StructureSection load='5wqw' size='340' side='right'caption='[[5wqw]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='5wqw' size='340' side='right'caption='[[5wqw]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wqw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clope Clope]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5azm 5azm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WQW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_str._13 Clostridium perfringens str. 13]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5azm 5azm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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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]] 1.76&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPE1231 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195102 CLOPE])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqw OCA], [http://pdbe.org/5wqw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wqw RCSB], [http://www.ebi.ac.uk/pdbsum/5wqw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqw ProSAT]</span></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=5wqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqw OCA], [https://pdbe.org/5wqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wqw RCSB], [https://www.ebi.ac.uk/pdbsum/5wqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqw ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8XL11_CLOPE Q8XL11_CLOPE]
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Bacterial autolysins can partially hydrolyze cell wall peptidoglycans into small sections to regulate cell separation/division and the growth phase. Clostridium perfringens autolysin (Acp) has an N-terminal cell wall-binding domain and a C-terminal catalytic domain with glucosaminidase activity that belongs to the glycoside hydrolase 73 family. Here, we determined the X-ray structure of the Acp catalytic domain (AcpCD) at 1.76 A resolution. AcpCD has a unique crescent-shaped structure, forming a deep groove for substrate-binding at the center of the protein. The modeling study of the enzyme/substrate complex demonstrated that the length of the substrate-binding groove is closely related to the glucosaminidase activity. Mutagenesis analysis showed that AcpCD likely adopts a neighboring-group mechanism for the catalytic reaction.
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Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain.,Tamai E, Sekiya H, Goda E, Makihata N, Maki J, Yoshida H, Kamitori S FEBS Lett. 2017 Jan;591(1):231-239. doi: 10.1002/1873-3468.12515. Epub 2016 Dec, 19. PMID:27926788<ref>PMID:27926788</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5wqw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Clope]]
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[[Category: Clostridium perfringens str. 13]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Goda, E]]
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[[Category: Goda E]]
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[[Category: Kamitori, S]]
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[[Category: Kamitori S]]
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[[Category: Maki, J]]
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[[Category: Maki J]]
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[[Category: Makihata, N]]
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[[Category: Makihata N]]
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[[Category: Sekiya, H]]
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[[Category: Sekiya H]]
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[[Category: Tamai, E]]
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[[Category: Tamai E]]
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[[Category: Yoshida, H]]
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[[Category: Yoshida H]]
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[[Category: Autolysin]]
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[[Category: Glycoside hydrolase 73 family]]
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[[Category: Hydrolase]]
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Current revision

X-ray structure of catalytic domain of autolysin from Clostridium perfringens

PDB ID 5wqw

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