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- PDB-5a6s: Crystal structure of the CTP1L endolysin reveals how its activity... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5a6s | ||||||
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Title | Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product | ||||||
![]() | (ENDOLYSIN) x 2 | ||||||
![]() | STRUCTURAL PROTEIN / ENDOLYSIN / SECONDARY TRANSLATION PRODUCT / BACTERIOPHAGE | ||||||
Function / homology | ![]() peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dunne, M. / Leicht, S. / Krichel, B. / Mertens, H.D.T. / Thompson, A. / Krijgsveld, J. / Svergun, D.I. / GomezTorres, N. / Garde, S. / Uetrecht, C. ...Dunne, M. / Leicht, S. / Krichel, B. / Mertens, H.D.T. / Thompson, A. / Krijgsveld, J. / Svergun, D.I. / GomezTorres, N. / Garde, S. / Uetrecht, C. / Narbad, A. / Mayer, M.J. / Meijers, R. | ||||||
![]() | ![]() Title: Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. Authors: Matthew Dunne / Stefan Leicht / Boris Krichel / Haydyn D T Mertens / Andrew Thompson / Jeroen Krijgsveld / Dmitri I Svergun / Natalia Gómez-Torres / Sonia Garde / Charlotte Uetrecht / Arjan ...Authors: Matthew Dunne / Stefan Leicht / Boris Krichel / Haydyn D T Mertens / Andrew Thompson / Jeroen Krijgsveld / Dmitri I Svergun / Natalia Gómez-Torres / Sonia Garde / Charlotte Uetrecht / Arjan Narbad / Melinda J Mayer / Rob Meijers / ![]() ![]() ![]() ![]() Abstract: Bacteriophages produce endolysins, which lyse the bacterial host cell to release newly produced virions. The timing of lysis is regulated and is thought to involve the activation of a molecular ...Bacteriophages produce endolysins, which lyse the bacterial host cell to release newly produced virions. The timing of lysis is regulated and is thought to involve the activation of a molecular switch. We present a crystal structure of the activated endolysin CTP1L that targets Clostridium tyrobutyricum, consisting of a complex between the full-length protein and an N-terminally truncated C-terminal cell wall binding domain (CBD). The truncated CBD is produced through an internal translation start site within the endolysin gene. Mutants affecting the internal translation site change the oligomeric state of the endolysin and reduce lytic activity. The activity can be modulated by reconstitution of the full-length endolysin-CBD complex with free CBD. The same oligomerization mechanism applies to the CD27L endolysin that targets Clostridium difficile and the CS74L endolysin that targets Clostridium sporogenes. When the CTP1L endolysin gene is introduced into the commensal bacterium Lactococcus lactis, the truncated CBD is also produced, showing that the alternative start codon can be used in other bacterial species. The identification of a translational switch affecting oligomerization presented here has implications for the design of effective endolysins for the treatment of bacterial infections. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95.8 KB | Display | ![]() |
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PDB format | ![]() | 72 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 464.1 KB | Display | ![]() |
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Full document | ![]() | 465 KB | Display | |
Data in XML | ![]() | 20.7 KB | Display | |
Data in CIF | ![]() | 31.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jfxS ![]() 2nw0S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 32877.180 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 9031.121 Da / Num. of mol.: 1 Fragment: TRUNCATED CELL WALL BINDING DOMAIN, RESIDUES 195-274 Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Non-polymers , 4 types, 485 molecules ![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-SO4 / | ||||
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#4: Chemical | #5: Chemical | ChemComp-1PE / | #6: Water | ChemComp-HOH / | |
-Details
Sequence details | THIS CHAIN IS A TRUNCATED CELL WALL BINDING DOMAIN THAT IS THE RESULT OF SECONDARY TRANSLATION ...THIS CHAIN IS A TRUNCATED CELL WALL BINDING DOMAIN THAT IS THE RESULT OF SECONDARY TRANSLATIO |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.62 % / Description: NONE |
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Crystal grow | Details: 5-10 % PEG 8000, 20 MM TRIS PH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Details: KB MIRRORS |
Radiation | Monochromator: SI 1 1 1 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. obs: 40146 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 8.2 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 9.6 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 8 % / Rmerge(I) obs: 0.75 / Mean I/σ(I) obs: 2.6 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 1JFX AND 2NW0 HYBRID MODEL Resolution: 1.9→19.9 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.943 / SU B: 2.55 / SU ML: 0.075 / Cross valid method: THROUGHOUT / ESU R: 0.11 / ESU R Free: 0.114 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.486 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→19.9 Å
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Refine LS restraints |
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