Diamond Publications - Search Results

Search Again...

These results only include publications that have been reviewed and processed by Diamond Light Source. To also view papers that have not yet been processed click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

One item found (0 items not approved).

Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography	Structure of the receptor-binding carboxy-terminal domain of the bacteriophage T5 L-shaped tail fibre with and without its intra-molecular chaperone Carmela Garcia-Doval , José Castón , Daniel Luque , Meritxell Granell , José Otero , Antonio Llamas-Saiz , Madalena Renouard , Pascale Boulanger , Mark Van Raaij Viruses 7, 6424 - 6440 DOI: 10.3390/v7122946 PMID: 26670244 Diamond Proposal Number(s): [3808] Open Access Show Abstract ▼ Abstract: Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970-1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 angstrom resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 angstrom structure solved by molecular replacement. The additional chaperone domain (residues 1263-1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition.	Dec 2015

Instruments / Technical Area

Publication Details

Published

Actions

I02-Macromolecular Crystallography

Structure of the receptor-binding carboxy-terminal domain of the bacteriophage T5 L-shaped tail fibre with and without its intra-molecular chaperone

Carmela Garcia-Doval , José Castón , Daniel Luque , Meritxell Granell , José Otero , Antonio Llamas-Saiz , Madalena Renouard , Pascale Boulanger , Mark Van Raaij

Viruses 7, 6424 - 6440

DOI: 10.3390/v7122946

PMID: 26670244

Diamond Proposal Number(s): [3808]