1yb0

<table><tr><td colspan='2'>[[1yb0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YB0 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1yb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb0 OCA], [http://pdbe.org/1yb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yb0 RCSB], [http://www.ebi.ac.uk/pdbsum/1yb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yb0 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

We report a structural and functional analysis of the lambda prophage Ba02 endolysin (PlyL) encoded by the Bacillus anthracis genome. We show that PlyL comprises two autonomously folded domains, an N-terminal catalytic domain and a C-terminal cell wall-binding domain. We determined the crystal structure of the catalytic domain; its three-dimensional fold is related to that of the cell wall amidase, T7 lysozyme, and contains a conserved zinc coordination site and other components of the catalytic machinery. We demonstrate that PlyL is an N-acetylmuramoyl-L-alanine amidase that cleaves the cell wall of several Bacillus species when applied exogenously. We show, unexpectedly, that the catalytic domain of PlyL cleaves more efficiently than the full-length protein, except in the case of Bacillus cereus, and using GFP-tagged cell wall-binding domain, we detected strong binding of the cell wall-binding domain to B. cereus but not to other species tested. We further show that a related endolysin (Ply21) from the B. cereus phage, TP21, shows a similar pattern of behavior. To explain these data, and the species specificity of PlyL, we propose that the C-terminal domain inhibits the activity of the catalytic domain through intramolecular interactions that are relieved upon binding of the C-terminal domain to the cell wall. Furthermore, our data show that (when applied exogenously) targeting of the enzyme to the cell wall is not a prerequisite of its lytic activity, which is inherently high. These results may have broad implications for the design of endolysins as therapeutic agents.

Structure and lytic activity of a Bacillus anthracis prophage endolysin.,Low LY, Yang C, Perego M, Osterman A, Liddington RC J Biol Chem. 2005 Oct 21;280(42):35433-9. Epub 2005 Aug 15. PMID:16103125<ref>PMID:16103125</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1yb0" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Liddington, R C]]

[[Category: Low, L Y]]

[[Category: Osterman, A]]

[[Category: Perego, M]]

[[Category: Yang, C]]

[[Category: Plyl]]