Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1

Anna Marie Davies; Renee Tata; Alison Snape; Brian J. Sutton; Paul R. Brown

doi:10.1016/j.biochi.2008.12.003

Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1

Anna Marie Davies, Renee Tata, Alison Snape, Brian J. Sutton, Paul R. Brown

Research output: Contribution to journal › Article › peer-review

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Abstract

Gene ACIAD1637 from Acinetobacter baylyi ADP1 encodes a 182 amino acid putative antibiotic resistance protein. The structure of this protein (termed acepita) has been solved in space group P-2 to 2.35 angstrom resolution. Acepita belongs to the GCN5-related N-acetyltransferase (GNAT) family, and contains the four sequence motifs conserved among family members. The structure of acepita is compared with that of pita, its homologue from Pseudomonas aeruginosa. Acepita has a similar substrate profile to pita and performs a similar function.

Original language	English
Pages (from-to)	484 - 489
Journal	Biochimie
Volume	91
Issue number	4
DOIs	https://doi.org/10.1016/j.biochi.2008.12.003
Publication status	Published - Apr 2009

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title = "Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1",

abstract = "Gene ACIAD1637 from Acinetobacter baylyi ADP1 encodes a 182 amino acid putative antibiotic resistance protein. The structure of this protein (termed acepita) has been solved in space group P-2 to 2.35 angstrom resolution. Acepita belongs to the GCN5-related N-acetyltransferase (GNAT) family, and contains the four sequence motifs conserved among family members. The structure of acepita is compared with that of pita, its homologue from Pseudomonas aeruginosa. Acepita has a similar substrate profile to pita and performs a similar function.",

author = "Davies, {Anna Marie} and Renee Tata and Alison Snape and Sutton, {Brian J.} and Brown, {Paul R.}",

year = "2009",

month = apr,

doi = "10.1016/j.biochi.2008.12.003",

language = "English",

volume = "91",

pages = "484 -- 489",

journal = "Biochimie",

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TY - JOUR

T1 - Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1

AU - Davies, Anna Marie

AU - Tata, Renee

AU - Snape, Alison

AU - Sutton, Brian J.

AU - Brown, Paul R.

PY - 2009/4

Y1 - 2009/4

N2 - Gene ACIAD1637 from Acinetobacter baylyi ADP1 encodes a 182 amino acid putative antibiotic resistance protein. The structure of this protein (termed acepita) has been solved in space group P-2 to 2.35 angstrom resolution. Acepita belongs to the GCN5-related N-acetyltransferase (GNAT) family, and contains the four sequence motifs conserved among family members. The structure of acepita is compared with that of pita, its homologue from Pseudomonas aeruginosa. Acepita has a similar substrate profile to pita and performs a similar function.

AB - Gene ACIAD1637 from Acinetobacter baylyi ADP1 encodes a 182 amino acid putative antibiotic resistance protein. The structure of this protein (termed acepita) has been solved in space group P-2 to 2.35 angstrom resolution. Acepita belongs to the GCN5-related N-acetyltransferase (GNAT) family, and contains the four sequence motifs conserved among family members. The structure of acepita is compared with that of pita, its homologue from Pseudomonas aeruginosa. Acepita has a similar substrate profile to pita and performs a similar function.

U2 - 10.1016/j.biochi.2008.12.003

DO - 10.1016/j.biochi.2008.12.003

M3 - Article

VL - 91

SP - 484

EP - 489

JO - Biochimie

JF - Biochimie

IS - 4

ER -

Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1

Abstract

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