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Yorodumi- SASDAD7: Structure of a complex between full length and truncated CTP1L en... -
+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDAD7 |
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Sample | Structure of a complex between full length and truncated CTP1L endolysin
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Function / homology | Glycosyl hydrolase family 25 (GH25) domain profile. / Glycoside hydrolase, family 25 / Glycosyl hydrolases family 25 / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / Glycoside hydrolase superfamily / lysozyme Function and homology information |
Biological species | Clostridium phage phiCTP1 (virus) |
Citation | Journal: J Biol Chem / Year: 2016 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. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Models
Model #255 | Type: mix / Software: CRYSOL / Chi-square value: 2.028 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #256 | Type: dummy / Software: DAMMIF / Radius of dummy atoms: 3.00 A / Chi-square value: 1.761 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Structure of a complex between full length and truncated CTP1L endolysin Specimen concentration: 1.00-4.00 |
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Buffer | Name: 20 mM HEPES / pH: 7.4 |
Entity #154 | Name: CTP1L / Type: protein / Description: EndolysinLysin / Formula weight: 32.839 / Source: Clostridium phage phiCTP1 / References: UniProt: D9ZNF3 Sequence: MGSSHHHHHH SSGLVPRGSH MKKIADISNL NGNVDVKLLF NLGYIGIIAK ASEGGTFVDK YYKQNYTNTK AQGKITGAYH FANFSTIAKA QQEANFFLNC IAGTTPDFVV LDLEQQCTGD ITDACLAFLN IVAKKFKCVV YCNSSFIKEH LNSKICAYPL WIANYGVATP ...Sequence: MGSSHHHHHH SSGLVPRGSH MKKIADISNL NGNVDVKLLF NLGYIGIIAK ASEGGTFVDK YYKQNYTNTK AQGKITGAYH FANFSTIAKA QQEANFFLNC IAGTTPDFVV LDLEQQCTGD ITDACLAFLN IVAKKFKCVV YCNSSFIKEH LNSKICAYPL WIANYGVATP AFTLWTKYAM WQFTEKGQVS GISGYIDFSY ITDEFIKYIK GEDEVENLVV YNDGADQRAA EYLADRLACP TINNARKFDY SNVKNVYAVG GNKEQYTSYL TTLIAGSTRY TTMQAVLDYI KNLK |
-Experimental information
Beam | Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm | |||||||||||||||||||||
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Detector | Name: Pilatus 1M-W / Pixsize x: 0.172 mm | |||||||||||||||||||||
Scan | Title: CTPL1 Endolysin / Measurement date: Mar 17, 2011 / Cell temperature: 20 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 821 /
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Result | D max: 13.8 / Type of curve: merged
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