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1yb0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1yb0 |SIZE=350|CAPTION= <scene name='initialview01'>1yb0</scene>, resolution 1.86Å | |PDB= 1yb0 |SIZE=350|CAPTION= <scene name='initialview01'>1yb0</scene>, resolution 1.86Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1yb0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yb0 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Perego, M.]] | [[Category: Perego, M.]] | ||
[[Category: Yang, C.]] | [[Category: Yang, C.]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: e c.3 5.1 28]] | [[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://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:01:09 2008'' |
Revision as of 22:01, 30 March 2008
| |||||||
| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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