Abstract:
:Computer analysis of the crystallographic structure of the A subunit of Escherichia coli heat-labile toxin (LT) was used to predict residues involved in NAD binding, catalysis and toxicity. Following site-directed mutagenesis, the mutants obtained could be divided into three groups. The first group contained fully assembled, non-toxic new molecules containing mutations of single amino acids such as Val-53-->Glu or Asp, Ser-63-->Lys, Val-97-->Lys, Tyr-104-->Lys or Asp, and Ser-114-->Lys or Glu. This group also included mutations in amino acids such as Arg-7, Glu-110 and Glu-112 that were already known to be important for enzymatic activity. The second group was formed by mutations that caused the collapse or prevented the assembly of the A subunit: Leu-41-->Phe, Ala-45-->Tyr or Glu, Val-53-->Tyr, Val-60-->Gly, Ser-68-->Pro, His-70-->Pro, Val-97-->Tyr and Ser-114-->Tyr. The third group contained those molecules that maintained a wild-type level of toxicity in spite of the mutations introduced: Arg-54-->Lys or Ala, Tyr-59-->Met, Ser-68-->Lys, Ala-72-->Arg, His or Asp and Arg-192-->Asn. The results provide a further understanding of the structure-function of the active site and new, non-toxic mutants that may be useful for the development of vaccines against diarrhoeal diseases.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Pizza M,Domenighini M,Hol W,Giannelli V,Fontana MR,Giuliani MM,Magagnoli C,Peppoloni S,Manetti R,Rappuoli Rdoi
10.1111/j.1365-2958.1994.tb01266.xsubject
Has Abstractpub_date
1994-10-01 00:00:00pages
51-60issue
1eissn
0950-382Xissn
1365-2958journal_volume
14pub_type
杂志文章abstract::Post-transcriptional repression of porin synthesis has emerged as a major function of Hfq-dependent, small non-coding RNAs (sRNAs). Many enterobacteria express OmpX-like porins, a family of outer membrane proteins whose physiological roles and structural properties have been studied intensively. While regulatory sRNAs...
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