5wqw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5wqw" [edit=sysop:move=sysop])
Line 7: Line 7:
<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=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>
<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=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>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
 +
 +
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>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5wqw" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 11:04, 1 February 2017

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

5wqw, resolution 1.76Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools