A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis

The FEBS Journal
Sook-Kyung KimJane E Ladner

Abstract

The Rv0948c gene from Mycobacterium tuberculosis H(37)R(v) encodes a 90 amino acid protein as the natural gene product with chorismate mutase (CM) activity. The protein, 90-MtCM, exhibits Michaelis-Menten kinetics with a k(cat) of 5.5+/-0.2s(-1) and a K(m) of 1500+/-100microm at 37 degrees C and pH7.5. The 2.0A X-ray structure shows that 90-MtCM is an all alpha-helical homodimer (Protein Data Bank ID: 2QBV) with the topology of Escherichia coli CM (EcCM), and that both protomers contribute to each catalytic site. Superimposition onto the structure of EcCM and the sequence alignment shows that the C-terminus helix3 is shortened. The absence of two residues in the active site of 90-MtCM corresponding to Ser84 and Gln88 of EcCM appears to be one reason for the low k(cat). Hence, 90-MtCM belongs to a subfamily of alpha-helical AroQ CMs termed AroQ(delta.) The CM gene (y2828) from Yersinia pestis encodes a 186 amino acid protein with an N-terminal signal peptide that directs the protein to the periplasm. The mature protein, *YpCM, exhibits Michaelis-Menten kinetics with a k(cat) of 70+/-5s(-1) and K(m) of 500+/-50microm at 37 degrees C and pH7.5. The 2.1A X-ray structure shows that *YpCM is an all alpha-helical protein, and function...Continue Reading

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Citations

Oct 24, 2009·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Mats OkvistUte Krengel
Jan 19, 2016·Journal of Molecular Biology·Steffi MunackUte Krengel
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Apr 11, 2018·Acta Crystallographica. Section F, Structural Biology Communications·Oluwatoyin A AsojoPeter J Myler
Oct 12, 2020·The Journal of Biological Chemistry·Jūratė Fahrig-KamarauskaitėPeter Kast
Feb 20, 2021·Chemical Communications : Chem Comm·Florian HubrichJennifer N Andexer
Jan 18, 2021·The Journal of Biological Chemistry·Jūrate Fahrig-KamarauskaitPeter Kast

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