Allosteric communication between alpha and beta subunits of tryptophan synthase: Modelling the open-closed transition of the alpha subunit

2006 ◽  
Vol 1764 (6) ◽  
pp. 1102-1109 ◽  
Author(s):  
Francesca Spyrakis ◽  
Samanta Raboni ◽  
Pietro Cozzini ◽  
Stefano Bettati ◽  
Andrea Mozzarelli
Keyword(s):  
Alpha Subunit ◽  
Beta Subunits ◽  
Tryptophan Synthase ◽  
Allosteric Communication

Mutational analysis of the functional domains of yeast K1 killer toxin

1991 ◽  
Vol 11 (1) ◽  
pp. 175-181
Author(s):  
H Zhu ◽  
H Bussey
Keyword(s):  
Cell Wall ◽  
Receptor Binding ◽  
Mutational Analysis ◽  
Killer Toxin ◽  
Alpha Subunit ◽  
Functional Domains ◽  
Beta Subunits ◽  
Channel Formation ◽  
Beta Glucan ◽  
Beta Toxin

To determine the functional domains of K1 killer toxin, we analyzed the phenotypes of a set of mutations throughout regions encoding the alpha- and beta-toxin subunits that allow secretion of mutant toxins. A range of techniques have been used to examine the ability of mutant toxins to bind to beta-glucan cell wall receptor and to form lethal ion channels. Our results indicate that both the alpha and beta subunits are involved in beta-glucan receptor binding. Defects in ion channel formation and toxin immunity are confined to the hydrophobic alpha subunit of the toxin.

scholarly journals Investigations into the post-translational modification and mechanism of isopenicillin N:acyl-CoA acyltransferase using electrospray mass spectrometry

1993 ◽  
Vol 294 (2) ◽  
pp. 357-363 ◽  
Author(s):  
R T Aplin ◽  
J E Baldwin ◽  
P L Roach ◽  
C V Robinson ◽  
C J Schofield
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
British Library ◽  
Beta Subunits ◽  
Post Translational Modification ◽  
Acetic Acids

Electrospray mass spectrometry (e.s.m.s.) was used to confirm the position of the post-translational cleavage of the isopenicillin N:acyl-CoA acyltransferase preprotein to give the alpha- and beta-subunits. The e.s.m.s. studies suggested partial modification of the alpha-subunit in vivo by exogenously added substituted acetic acids. E.s.m.s. has also allowed the observation in vitro of the transfer of the acyl group from several acyl-CoAs to the beta-subunit. N.m.r. data for the CoA species have been deposited as Supplementary Publication SUP 500173 (2 pages) at the British Library Document Supply Centre (DSC), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, from whom copies can be obtained on the terms indicated in Biochem. J. (1993) 289, 9.

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