4DQN

Crystal structure of the branched-chain aminotransferase from Streptococcus mutans

Summary for 4DQN

• Entry DOI: 10.2210/pdb4dqn/pdb
• Descriptor: Putative branched-chain amino acid aminotransferase IlvE (2 entities in total)
• Functional Keywords: aminotransferase, transferase
• Biological source: Streptococcus mutans
• Total number of polymer chains: 1
• Total formula weight: 38053.66

Authors

Ruan, J.,Li, S.T. (deposition date: 2012-02-16, release date: 2013-01-02, Last modification date: 2023-11-08)

Primary citation

Ruan, J.,Hu, J.,Yin, A.H.,Wu, W.Q.,Cong, X.Z.,Feng, X.T.,Li, S.T.
Structure of the branched-chain aminotransferase from Streptococcus mutans
Acta Crystallogr.,Sect.D, 68:996-1002, 2012

PubMed Abstract: The branched-chain amino-acid aminotransferase from Streptococcus mutans (SmIlvE) was recombinantly expressed in Escherichia coli with high yield. An effective purification protocol was established. A bioactivity assay indicated that SmIlvE had aminotransferase activity. The specific activity of SmIlvE towards amino-acid substrates was found to be as follows (in descending order): Ile > Leu > Val > Trp > Gly. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG 3350 as the primary precipitant. The structure of SmIlvE was solved at 1.97 Å resolution by the molecular-replacement method. Comparison with structures of homologous proteins enabled the identification of conserved structural elements that might play a role in substrate binding. Further work is needed to confirm the interaction between SmIlvE and its substrates by determining the structures of their complexes.

PubMed: 22868765
DOI: 10.1107/S0907444912018446

Experimental method

X-RAY DIFFRACTION (1.97 Å)