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PDBsum entry 4my5
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PDB id:
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Transferase
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Title:
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Crystal structure of the aromatic amino acid aminotransferase from streptococcus mutants
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Structure:
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Putative amino acid aminotransferase. Chain: a, d, b, c. Engineered: yes
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Source:
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Streptococcus mutans. Organism_taxid: 210007. Strain: atcc 700610 / ua159. Gene: smu_24. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.19Å
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R-factor:
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0.193
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R-free:
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0.239
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Authors:
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X.Cong,X.Li,J.Ge,Y.Feng,X.Feng,S.Li
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Key ref:
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X.Cong
et al.
(2019).
Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans.
Acta Crystallogr F Struct Biol Commun,
75,
141-146.
PubMed id:
DOI:
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Date:
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27-Sep-13
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Release date:
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01-Oct-14
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PROCHECK
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Headers
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References
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Q8DWM1
(Q8DWM1_STRMU) -
Aminotransferase from Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
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Seq:
Struc:
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391 a.a.
390 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Acta Crystallogr F Struct Biol Commun
75:141-146
(2019)
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PubMed id:
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Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans.
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X.Cong,
X.Li,
S.Li.
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ABSTRACT
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Streptococcus mutans, a facultatively aerobic and Gram-positive bacterium, is
the primary causative agent of dental caries and contributes to the multispecies
biofilm known as dental plaque. In this study, the aromatic-amino-acid
aminotransferase from Streptococcus mutans (SmAroAT) was recombinantly expressed
in Escherichia coli. An effective purification protocol was established. The
recombinant protein was crystallized using the hanging-drop vapor-diffusion
method with PEG 3350 as the primary precipitant. The crystal structure of
SmAroAT was solved at 2.2 Å resolution by the molecular-replacement method.
Structural analysis indicated that the proteins of the aromatic-amino-acid
aminotransferase family have conserved structural elements that might play a
role in substrate binding. These results may help in obtaining a better
understanding of the catabolism and biosynthesis of aromatic amino acids.
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Links
