Rv0802c from Mycobacterium tuberculosis

The first structure of a succinyltransferase with the GNAT fold

Matthew W. Vetting, James C. Errey, John S. Blanchard

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Gene rv0802c from Mycobacterium tuberculosis encodes a 218-amino-acid protein and is annotated as a hypothetical protein with homology to GCN5-related N-acetyltransferases. The structure of Rv0802c was determined in an unliganded form to 2.0 Å resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+: citrate2 complex. The structure confirms that Rv0802c exhibits the GCN5-related N-acetyltransferase fold and revealed a tetramer composed of a dimer of dimers with approximate 222 symmetry. In addition, a bound acetate ion indicated that Rv0802c may utilize a unique acyl donor for the family. The subsequent determination of the structure of Rv0802c in complex with succinyl-CoA to 2.3 Å resolution suggests that Rv0802c is the first known GCN5-related N-acetyltransferase family member to utilize succinyl-CoA as a substrate.

Original languageEnglish (US)
Pages (from-to)978-985
Number of pages8
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number11
DOIs
StatePublished - 2008

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tuberculosis
Acetyltransferases
Mycobacterium tuberculosis
dimers
proteins
Dimers
samarium
homology
Samarium
genes
amino acids
acetates
Proteins
Acetates
symmetry
Genes
wavelengths
Ions
Amino Acids
Wavelength

Keywords

  • GCN5-related N-acetyltransferases
  • Mycobacterium tuberculosis
  • Rv0802c

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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abstract = "Gene rv0802c from Mycobacterium tuberculosis encodes a 218-amino-acid protein and is annotated as a hypothetical protein with homology to GCN5-related N-acetyltransferases. The structure of Rv0802c was determined in an unliganded form to 2.0 {\AA} resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+: citrate2 complex. The structure confirms that Rv0802c exhibits the GCN5-related N-acetyltransferase fold and revealed a tetramer composed of a dimer of dimers with approximate 222 symmetry. In addition, a bound acetate ion indicated that Rv0802c may utilize a unique acyl donor for the family. The subsequent determination of the structure of Rv0802c in complex with succinyl-CoA to 2.3 {\AA} resolution suggests that Rv0802c is the first known GCN5-related N-acetyltransferase family member to utilize succinyl-CoA as a substrate.",
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T2 - The first structure of a succinyltransferase with the GNAT fold

AU - Vetting, Matthew W.

AU - Errey, James C.

AU - Blanchard, John S.

PY - 2008

Y1 - 2008

N2 - Gene rv0802c from Mycobacterium tuberculosis encodes a 218-amino-acid protein and is annotated as a hypothetical protein with homology to GCN5-related N-acetyltransferases. The structure of Rv0802c was determined in an unliganded form to 2.0 Å resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+: citrate2 complex. The structure confirms that Rv0802c exhibits the GCN5-related N-acetyltransferase fold and revealed a tetramer composed of a dimer of dimers with approximate 222 symmetry. In addition, a bound acetate ion indicated that Rv0802c may utilize a unique acyl donor for the family. The subsequent determination of the structure of Rv0802c in complex with succinyl-CoA to 2.3 Å resolution suggests that Rv0802c is the first known GCN5-related N-acetyltransferase family member to utilize succinyl-CoA as a substrate.

AB - Gene rv0802c from Mycobacterium tuberculosis encodes a 218-amino-acid protein and is annotated as a hypothetical protein with homology to GCN5-related N-acetyltransferases. The structure of Rv0802c was determined in an unliganded form to 2.0 Å resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+: citrate2 complex. The structure confirms that Rv0802c exhibits the GCN5-related N-acetyltransferase fold and revealed a tetramer composed of a dimer of dimers with approximate 222 symmetry. In addition, a bound acetate ion indicated that Rv0802c may utilize a unique acyl donor for the family. The subsequent determination of the structure of Rv0802c in complex with succinyl-CoA to 2.3 Å resolution suggests that Rv0802c is the first known GCN5-related N-acetyltransferase family member to utilize succinyl-CoA as a substrate.

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