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| | [[Image:1yb0.gif|left|200px]] | | [[Image:1yb0.gif|left|200px]] |
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| | {{STRUCTURE_1yb0| PDB=1yb0 | SCENE= }} | | {{STRUCTURE_1yb0| PDB=1yb0 | SCENE= }} |
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| - | '''Structure of PlyL'''
| + | ===Structure of PlyL=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16103125}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16103125 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16103125}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: N-acetylmuramoyl-l-alanine amidase]] | | [[Category: N-acetylmuramoyl-l-alanine amidase]] |
| | [[Category: Plyl]] | | [[Category: Plyl]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:05:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:38:35 2008'' |
Revision as of 15:38, 28 July 2008
Template:STRUCTURE 1yb0
Structure of PlyL
Template:ABSTRACT PUBMED 16103125
About this Structure
1YB0 is a Single protein structure of sequence from Bacillus anthracis. 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
Page seeded by OCA on Mon Jul 28 18:38:35 2008
