• Login
    View Item 
    •   Home
    • iBEST Institute of Biomedical and Environmental Science and Technology - to April 2016
    • Cell and Cryobiology Research Group
    • View Item
    •   Home
    • iBEST Institute of Biomedical and Environmental Science and Technology - to April 2016
    • Cell and Cryobiology Research Group
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UOBREPCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournalDepartmentThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournalDepartment

    My Account

    LoginRegister

    About

    AboutLearning ResourcesResearch Graduate SchoolResearch InstitutesUniversity Website

    Statistics

    Display statistics

    A network of dynamically conserved residues deciphers the motions of maltose transporter

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Lukman, Suryani
    Grant, Guy H.
    Affiliation
    University of Cambridge
    Issue Date
    2009-08-15
    
    Metadata
    Show full item record
    Abstract
    The maltose transporter of Escherichia coli is a member of the ATP-binding cassette (ABC) transporter superfamily. The crystal structures of maltose transporter MalK have been determined for distinct conformations in the presence and absence of the ligand ATP, and other interacting proteins. Using the distinct MalK structures, normal mode analysis was performed to understand the dynamics behavior of the system. A network of dynamically important residues was obtained from the normal mode analysis and the analysis of point mutation on the normal modes. Our results suggest that the intradomain rotation occurs earlier than the interdomain rotation during the maltose-binding protein (MBP)-driven conformational changes of MalK. We inquire if protein motion and functional-driven evolutionary conservation are related. The sequence conservation of MalK was analyzed to derive a network of evolutionarily important residues. There are highly significant correlations between protein sequence and protein dynamics in many regions on the maltose transporter MalK, suggesting a link between the protein evolution and dynamics. The significant overlaps between the network of dynamically important residues and the network of evolutionarily important residues form a network of dynamically conserved residues.
    Citation
    Lukman, S., Grant G.H. (2009) 'A network of dynamically conserved residues deciphers the motions of maltose transporter' Proteins 76 (3):588-97
    Publisher
    Wiley-Blackwell
    Journal
    Proteins
    URI
    http://hdl.handle.net/10547/227130
    DOI
    10.1002/prot.22372
    PubMed ID
    19274733
    Additional Links
    http://onlinelibrary.wiley.com/doi/10.1002/prot.22372/abstract;jsessionid=A6EBA2CF3DF51272983A9265E1620827.f01t04
    Type
    Article
    Language
    en
    ISSN
    1097-0134
    ae974a485f413a2113503eed53cd6c53
    10.1002/prot.22372
    Scopus Count
    Collections
    Cell and Cryobiology Research Group

    entitlement

     
    DSpace software (copyright © 2002 - 2021)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.