Abstract
SyrC, a component of the multienzyme system of syringomycin biosynthesis, has been shown to shuttle Thr/4-Cl-Thr between the thiolation domains SyrBl-Tl and Syr-E-T8,9 by transiently linking it to Cys224 in the enzyme active site. We present data on the structure-function relationship in vivo of this protein and an in silico model of its three-dimensional structure. The biosynthetic activity of SyrC was not influenced when either Asp348 or His376 that together with Cys224 form a putative catalytic triad, were replaced with Ala, but it was abolished by the exchange Cys224 with Ser. The presence of the FLAG peptide on either the N- or C-terminus of the protein did not affect activity, whereas the deletion of the first 16 amino acids at the N-terminus or the insertion of Maltose Binding Protein abolished the production of syringomycin. We present the model of the three-dimensional structure of SyrC suggesting a homodimeric structure for the protein and biochemical data that are supportive of this model.
| Original language | English |
|---|---|
| Pages (from-to) | 201-207 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 364 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 14 Dec 2007 |
| Externally published | Yes |
Cite this
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Mutational analysis and homology modelling of SyrC, the aminoacyltransferase in the biosynthesis of syringomycin. / Fullone, Maria Rosaria; Paiardini, Alessandro; Gross, Dennis C.; Lu, Shi-En; Fiore, Alberto; Grgurina, Ingeborg.
In: Biochemical and Biophysical Research Communications, Vol. 364, No. 2, 14.12.2007, p. 201-207.Research output: Contribution to journal › Article
TY - JOUR
T1 - Mutational analysis and homology modelling of SyrC, the aminoacyltransferase in the biosynthesis of syringomycin
AU - Fullone, Maria Rosaria
AU - Paiardini, Alessandro
AU - Gross, Dennis C.
AU - Lu, Shi-En
AU - Fiore, Alberto
AU - Grgurina, Ingeborg
PY - 2007/12/14
Y1 - 2007/12/14
N2 - SyrC, a component of the multienzyme system of syringomycin biosynthesis, has been shown to shuttle Thr/4-Cl-Thr between the thiolation domains SyrBl-Tl and Syr-E-T8,9 by transiently linking it to Cys224 in the enzyme active site. We present data on the structure-function relationship in vivo of this protein and an in silico model of its three-dimensional structure. The biosynthetic activity of SyrC was not influenced when either Asp348 or His376 that together with Cys224 form a putative catalytic triad, were replaced with Ala, but it was abolished by the exchange Cys224 with Ser. The presence of the FLAG peptide on either the N- or C-terminus of the protein did not affect activity, whereas the deletion of the first 16 amino acids at the N-terminus or the insertion of Maltose Binding Protein abolished the production of syringomycin. We present the model of the three-dimensional structure of SyrC suggesting a homodimeric structure for the protein and biochemical data that are supportive of this model.
AB - SyrC, a component of the multienzyme system of syringomycin biosynthesis, has been shown to shuttle Thr/4-Cl-Thr between the thiolation domains SyrBl-Tl and Syr-E-T8,9 by transiently linking it to Cys224 in the enzyme active site. We present data on the structure-function relationship in vivo of this protein and an in silico model of its three-dimensional structure. The biosynthetic activity of SyrC was not influenced when either Asp348 or His376 that together with Cys224 form a putative catalytic triad, were replaced with Ala, but it was abolished by the exchange Cys224 with Ser. The presence of the FLAG peptide on either the N- or C-terminus of the protein did not affect activity, whereas the deletion of the first 16 amino acids at the N-terminus or the insertion of Maltose Binding Protein abolished the production of syringomycin. We present the model of the three-dimensional structure of SyrC suggesting a homodimeric structure for the protein and biochemical data that are supportive of this model.
U2 - 10.1016/j.bbrc.2007.09.116
DO - 10.1016/j.bbrc.2007.09.116
M3 - Article
VL - 364
SP - 201
EP - 207
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -