1yb0
From Proteopedia
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| - | [[Image:1yb0.gif|left|200px]] | + | [[Image:1yb0.gif|left|200px]] |
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| - | '''Structure of PlyL''' | + | {{Structure |
| + | |PDB= 1yb0 |SIZE=350|CAPTION= <scene name='initialview01'>1yb0</scene>, resolution 1.86Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of PlyL''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YB0 is a [ | + | 1YB0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YB0 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16103125 16103125] |
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: plyl]] | [[Category: plyl]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:35 2008'' |
Revision as of 13:20, 20 March 2008
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| , resolution 1.86Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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