In vitro folding pathway of phage P22 tailspike protein

Biochemistry ◽  
1991 ◽  
Vol 30 (26) ◽  
pp. 6598-6604 ◽  
Author(s):  
Albert Fuchs ◽  
Claudia Seiderer ◽  
Robert Seckler
Keyword(s):  
Folding Pathway ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro

1989 ◽  
Vol 264 (20) ◽  
pp. 11750-11753
Author(s):  
R Seckler ◽  
A Fuchs ◽  
J King ◽  
R Jaenicke
Keyword(s):  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.

1996 ◽  
Vol 93 (20) ◽  
pp. 10584-10588 ◽  
Author(s):  
S. Steinbacher ◽  
U. Baxa ◽  
S. Miller ◽  
A. Weintraub ◽  
R. Seckler ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Antigen Receptors ◽  
O Antigen ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals An essential serotype recognition pocket on phage P22 tailspike protein forces Salmonella enterica serovar Paratyphi A O-antigen fragments to bind as nonsolution conformers

Glycobiology ◽  
2013 ◽  
Vol 23 (4) ◽  
pp. 486-494 ◽  
Author(s):  
Dorothee Andres ◽  
Ulrich Gohlke ◽  
Nina K Broeker ◽  
Stefan Schulze ◽  
Wolfgang Rabsch ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
O Antigen ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals Stem Mutants in the N-terminal Domain of the Phage P22 Tailspike Protein

2013 ◽  
Vol 2 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Chris Palmer ◽  
Jeremie Williams ◽  
Dexter Dean ◽  
Sam Johnson ◽  
Hongzhuan Wu ◽  
...  
Keyword(s):  
Terminal Domain ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins

2009 ◽  
Vol 419 (3) ◽  
pp. 595-602 ◽  
Author(s):  
Tawnya Webber ◽  
Sarsati Gurung ◽  
Justin Saul ◽  
Trenton Baker ◽  
Michelle Spatara ◽  
...  
Keyword(s):  
Hydrophobic Interactions ◽  
Critical Role ◽  
Oligomeric Proteins ◽  
C Terminus ◽  
Monomeric Proteins ◽  
P22 Tailspike ◽  
Tailspike Protein ◽  
Oligomerization Domain

TSP (P22 tailspike protein) is a well-established model system for studying the folding and assembly of oligomeric proteins, and previous studies have documented both in vivo and in vitro folding intermediates using this protein. Especially important is the C-terminus of TSP, which plays a critical role in the assembly and maturation of the protrimer intermediate to its final trimeric form. In the present study, we show that by grafting the C-terminus of TSP on to the monomeric MBP (maltose-binding protein), the resulting chimaera (MBP-537) is a trimeric protein. Moreover, Western blot studies (using an anti-TSP antibody) indicate that the TSP C-terminus in the MBP-537 chimaera has the same conformation as the native TSP. The oligomerization of the MBP-537 chimaera appears to involve hydrophobic interactions and a refolding sequence, both of which are analogous to the native TSP. These results underscore the importance of the TSP C-terminus in the assembly of the mature trimer and demonstrate its potential utility as a model to study the folding and assembly of the TSP C-terminus in isolation.

scholarly journals Enthalpic Barriers to the Hydrophobic Binding of Oligosaccharides to Phage P22 Tailspike Protein†

Biochemistry ◽  
2001 ◽  
Vol 40 (17) ◽  
pp. 5144-5150 ◽  
Author(s):  
Ulrich Baxa ◽  
Alan Cooper ◽  
Andrej Weintraub ◽  
Wolfgang Pfeil ◽  
Robert Seckler
Keyword(s):  
Hydrophobic Binding ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals Multiple Solvent Crystal Structures of phage P22 tailspike protein: An analysis of binding site hot spots and surface hydration

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Patrick Donohue ◽  
Mychal Smith ◽  
Nina Broeker ◽  
Carolin Doering ◽  
Carla Mattos ◽  
...  
Keyword(s):  
Binding Site ◽  
Crystal Structures ◽  
Hot Spots ◽  
Surface Hydration ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein
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