1yb0
From Proteopedia
(New page: 200px<br /><applet load="1yb0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yb0, resolution 1.86Å" /> '''Structure of PlyL'''...) |
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| - | [[Image:1yb0.gif|left|200px]]<br /><applet load="1yb0" size=" | + | [[Image:1yb0.gif|left|200px]]<br /><applet load="1yb0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yb0, resolution 1.86Å" /> | caption="1yb0, resolution 1.86Å" /> | ||
'''Structure of PlyL'''<br /> | '''Structure of PlyL'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report a structural and functional analysis of the lambda prophage Ba02 | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YB0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] with ZN and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YB0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YB0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
| - | [[Category: Low, L | + | [[Category: Low, L Y.]] |
[[Category: Osterman, A.]] | [[Category: Osterman, A.]] | ||
[[Category: Perego, M.]] | [[Category: Perego, M.]] | ||
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[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| - | [[Category: e | + | [[Category: e c.3 5.1 28]] |
[[Category: n-acetylmuramoyl-l-alanine amidase]] | [[Category: n-acetylmuramoyl-l-alanine amidase]] | ||
[[Category: plyl]] | [[Category: plyl]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:30 2008'' |
Revision as of 14:03, 21 February 2008
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Structure of PlyL
Overview
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.
About this Structure
1YB0 is a Single protein structure of sequence from Bacillus anthracis with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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