ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Temperature Dependence of the Structure of the Substrate and Active Site of the Thermus thermophilus Chorismate Mutase E·S Complex

View Author Information
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106
Cite this: Biochemistry 2006, 45, 28, 8562–8567
Publication Date (Web):June 27, 2006
https://doi.org/10.1021/bi0604227
Copyright © 2006 American Chemical Society

    Article Views

    195

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options
    Supporting Info (2)»

    Abstract

    Abstract Image

    Molecular dynamics (MD) simulations of Thermus thermophilus chorismate mutase substrate complex (TtCM·S) have been carried out at 298 K, 333 K, and the temperature of optimum activity:  343 K. The enzyme exists as trimeric subunits with active sites shared between two neighboring subunits. Two features distinguish intersubunit linkages of the thermophilic and mesophilic enzyme Bacillus subtilis chorismate mutase substrate complex (BsCM·S):  (i) electrostatic interactions by intersubunit ion pairs (Arg3-Glu40*/41, Arg76-Glu51* and Arg69*-Asp101, residues labeled with an asterisk are from the neighboring subunit) in the TtCM·S are not present in the structure of the BsCM·S; and (ii) replacement of polar residues with short and nonpolar residues in the interstices of the TtCM·S tighten the intersubunit hydrophobic interactions compared to BsCM·S. Concerning the active site, electrostatic interactions of the critically placed Arg6 and Arg63* with the two carboxylates of chorismate place the latter in a reactive conformation to spontaneously undergo a Claisen rearrangement. The optimum geometry at the active site has the CZ atoms of the two arginines 11 Å apart. With a decrease in temperature, Arg63* moves toward Arg6 and the average conformation structure of chorismate moves further away from the reactive ground state conformation. This movement is due to the decrease in distance separating the electrostatic (in the main) and hydrophobic interacting pairs holding the two subunits together.

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

     Supported by the National Institutes of Health Grant 5R37DK9174-41.

    *

     To whom correspondence should be addressed. Tel:  (805) 893-2044. Fax:  (805) 893-2229. E-mail:  [email protected].

    Supporting Information Available

    ARTICLE SECTIONS
    Jump To

    The Stability of Intersubunit Interactions for the Thermus thermophilus Chorismate Mutase is available free of charge via the Internet at http://pubs.acs.org.

    Terms & Conditions

    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    This article is cited by 3 publications.

    1. Françoise Hervé, Nicolae Ghinea, Philippe D’Athis, Pierre-Alain Carrupt and Jean-Michel Scherrmann . Covalent Modifications of Antitetanus F(ab′)2 Fragments with Natural and Synthetic Polyamines and Their Effects on the Antibody Endocytosis in Cultured HL60 Cells. Bioconjugate Chemistry 2008, 19 (8) , 1543-1555. https://doi.org/10.1021/bc800045x
    2. Liangxu Xie, Mingjun Yang, Zhe-Ning Chen. Understanding the entropic effect in chorismate mutase reaction catalyzed by isochorismate-pyruvate lyase from Pseudomonas aeruginosa (PchB). Catalysis Science & Technology 2019, 9 (4) , 957-965. https://doi.org/10.1039/C8CY02123F
    3. Xiaodong Zhang, Swarnalatha Y. Reddy, Thomas C. Bruice. Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase. Proceedings of the National Academy of Sciences 2007, 104 (3) , 745-749. https://doi.org/10.1073/pnas.0610126104

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect