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Crystal Structures of Cobalamin-Independent Methionine Synthase (MetE) from Streptococcus mutans: A Dynamic Zinc-Inversion Model

  1. Author:
    Fu, T. M.
    Almqvist, J.
    Liang, Y. H.
    Li, L. F.
    Huang, Y. F.
    Su, X. D.

  2. Author Address

    [Almqvist, J; Huang, YF] Swedish Univ Agr Sci, Dept Mol Biol, Uppsala Biomed Ctr, S-75124 Uppsala, Sweden. [Fu, TM; Li, LF; Su, XD] Peking Univ, State Key Lab Prot & Plant Gene Res, Sch Life Sci, Beijing 100871, Peoples R China. [Almqvist, J] Stanford Univ, Dept Mol & Cellular Physiol, Sch Med, Stanford, CA 94305 USA. [Liang, YH] NCI, Frederick, MD 21702 USA.;Huang, YF (reprint author), Swedish Univ Agr Sci, Dept Mol Biol, Uppsala Biomed Ctr, POB 590, S-75124 Uppsala, Sweden;yafei.huang@molbio.slu.se xdsu@pku.edu.cn
    1. Year: 2011
    2. Date: Sep
  2. Journal: Journal of Molecular Biology
    1. 412
    2. 4
    3. Pages: 688-697
  4. Type of Article: Article
  5. ISSN: 0022-2836
  1. Abstract:

    Cobalamin-independent methionine synthase (MetE) catalyzes the direct transfer of a methyl group from methyltetrahydrofolate to L-homocysteine to form methionine. Previous studies have shown that the MetE active site coordinates a zinc atom, which is thought to act as a Lewis acid and plays a role in the activation of thiol. Extended X-ray absorption fine structure studies and mutagenesis experiments identified the zinc-binding site in MetE from Escherichia coli. Further structural investigations of MetE from Thermotoga maritima lead to the proposition of two models: "induced fit" and "dynamic equilibrium", to account for the catalytic mechanisms of MetE. Here, we present crystal structures of oxidized and zinc-replete MetE from Streptococcus mutans at the physiological pH. The structures reveal that zinc is mobile in the active center and has the possibility to invert even in the absence of homocysteine. These structures provide evidence for the dynamic equilibrium model. (C) 2011 Elsevier Ltd. All rights

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External Sources

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  2. DOI: 10.1016/j.jmb.2011.08.005
  3. View record in Web of Science®
  4. WOS: 000295496500012

Library Notes

  1. Fiscal Year: FY2011-2012
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