Biochemical and biophysical research communications, 2019-09, Vol.517 (3), p.399-406
2019
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- Autor(en) / Beteiligte
- Titel
- Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatis ATCC 19420
- Ist Teil von
- Biochemical and biophysical research communications, 2019-09, Vol.517 (3), p.399-406
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2019
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Mycobacterium smegmatis is a good model for studying the physiology and pathogenesis of Mycobacterium tuberculosis due to its genetic similarity. As methionine biosynthesis exists only in microorganisms, the enzymes involved in methionine biosynthesis can be a potential target for novel antibiotics. Homoserine O-acetyltransferase from M. smegmatis (MsHAT) catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine. To investigate the molecular mechanism of MsHAT, we determined its crystal structure in apo-form and in complex with either CoA or homoserine and revealed the substrate binding mode of MsHAT. A structural comparison of MsHAT with other HATs suggests that the conformation of the α5 to α6 region might influence the shape of the dimer. In addition, the active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HATs. •Crystal structures of Homoserine O-acetyltransferase from Mycobacterium smegmatis was determined.•The first complex structure with either CoA and homoserine elucidated detailed substrate binding mode of MsHAT.•We proposed that the different conformation of HATs might determine its dimer formation and its substrate binding affinity.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0006-291XeISSN: 1090-2104DOI: 10.1016/j.bbrc.2019.07.117Titel-ID: cdi_proquest_miscellaneous_2268574772
- Format
- –
- Schlagworte
- Acetyl Coenzyme A - chemistry, Acetyl Coenzyme A - metabolism, Acetyltransferases - chemistry, Acetyltransferases - genetics, Acetyltransferases - metabolism, Amino Acid Sequence, Antibiotics, Apoproteins - chemistry, Apoproteins - genetics, Apoproteins - metabolism, Bacterial Proteins - chemistry, Bacterial Proteins - genetics, Bacterial Proteins - metabolism, Catalytic Domain, Cloning, Molecular, Crystal structure, Crystallography, X-Ray, Escherichia coli - genetics, Escherichia coli - metabolism, Gene Expression, Genetic Vectors - chemistry, Genetic Vectors - metabolism, Haemophilus influenzae - chemistry, Haemophilus influenzae - enzymology, Haemophilus influenzae - genetics, Homoserine - chemistry, Homoserine - metabolism, Homoserine O-acetyltransferase, Kinetics, Leptospira interrogans - chemistry, Leptospira interrogans - enzymology, Leptospira interrogans - genetics, Models, Molecular, Mycobacteriaceae - chemistry, Mycobacteriaceae - enzymology, Mycobacteriaceae - genetics, Mycobacterium abscessus - chemistry, Mycobacterium abscessus - enzymology, Mycobacterium abscessus - genetics, Mycobacterium smegmatis, Mycobacterium smegmatis - chemistry, Mycobacterium smegmatis - enzymology, Mycobacterium smegmatis - genetics, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Recombinant Proteins - metabolism, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity