6T84

crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.174 
  • R-Value Observed: 0.175 

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This is version 1.1 of the entry. See complete history. 


Literature

The crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA, reveals an atypical fold.

Ung, K.L., Alsarraf, H.M.A.B., Kremer, L., Blaise, M.

(2020) Proteins 88: 809-815

  • DOI: https://doi.org/10.1002/prot.25863
  • Primary Citation of Related Structures:  
    6T84

  • PubMed Abstract: 

    Trehalose monomycolate (TMM) represents an essential element of the mycobacterial envelope. While synthesized in the cytoplasm, TMM is transported across the inner membrane by MmpL3 but, little is known regarding the MmpL3 partners involved in this process. Recently, the TMM transport factor A (TtfA) was found to form a complex with MmpL3 and to participate in TMM transport, although its biological role remains to be established. Herein, we report the crystal structure of the Mycobacterium smegmatis TtfA core domain. The phylogenetic distribution of TtfA homologues in non-mycolate containing bacteria suggests that TtfA may exert additional functions.

    • Organizational Affiliation: 

    Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, Montpellier, France.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Uncharacterized protein187Mycolicibacterium smegmatis MC2 155Mutation(s): 0 
Gene Names: MSMEG_0736
UniProt
Find proteins for A0QQF4 (Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155))
Explore A0QQF4 
Go to UniProtKB:  A0QQF4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0QQF4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.174 
  • R-Value Observed: 0.175 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.24α = 90
b = 70.09β = 90
c = 86.01γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
AutoSolphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

  • Released Date: 2019-12-25 
    • Deposition Author(s): Blaise, M.
Funding OrganizationLocationGrant Number
French National Research AgencyFranceANR-17-CE11-0008-01

Revision History  (Full details and data files)

  • Version 1.0: 2019-12-25
    Type: Initial release
  • Version 1.1: 2020-05-27
    Changes: Database references