6YIR

Crystal structure of Bacillus subtilis MsmX ATPase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.68 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.

Leisico, F.Godinho, L.M.Goncalves, I.C.Silva, S.P.Carneiro, B.Romao, M.J.Santos-Silva, T.de Sa-Nogueira, I.

(2020) Sci Rep 10: 19564-19564

  • DOI: https://doi.org/10.1038/s41598-020-76444-0
  • Primary Citation of Related Structures:  
    6YIR

  • PubMed Abstract: 

    ATP-binding cassette (ABC) type I importers are widespread in bacteria and play a crucial role in its survival and pathogenesis. They share the same modular architecture comprising two intracellular nucleotide-binding domains (NBDs), two transmembrane domains (TMDs) and a substrate-binding protein. The NBDs bind and hydrolyze ATP, thereby generating conformational changes that are coupled to the TMDs and lead to substrate translocation. A group of multitask NBDs that are able to serve as the cellular motor for multiple sugar importers was recently discovered. To understand why some ABC importers share energy-coupling components, we used the MsmX ATPase from Bacillus subtilis as a model for biological and structural studies. Here we report the first examples of functional hybrid interspecies ABC type I importers in which the NBDs could be exchanged. Furthermore, the first crystal structure of an assigned multitask NBD provides a framework to understand the molecular basis of the broader specificity of interaction with the TMDs.


  • Organizational Affiliation

    XTAL - Macromolecular Crystallography Laboratory, UCIBIO, Departamento de Química, Faculdade de Ciências E Tecnologia, Universidade NOVA de Lisboa, Quinta da Torre, 2829-516, Caparica, Portugal.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Oligosaccharides import ATP-binding protein MsmX373Bacillus subtilis subsp. subtilis str. 168Mutation(s): 1 
Gene Names: msmXyxkGBSU38810
EC: 7.5.2
UniProt
Find proteins for P94360 (Bacillus subtilis (strain 168))
Explore P94360 
Go to UniProtKB:  P94360
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP94360
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.68 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.200 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.758α = 90
b = 94.247β = 90
c = 132.263γ = 90
Software Package:
Software NamePurpose
MxCuBEdata collection
XDSdata reduction
STARANISOdata scaling
Aimlessdata scaling
ARP/wARPmodel building
Cootmodel building
PHASERphasing
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Fundacao para a Ciencia e a TecnologiaPortugalPTDC/BIA-MIC/30696/2017

Revision History  (Full details and data files)

  • Version 1.0: 2020-11-18
    Type: Initial release
  • Version 1.1: 2020-11-25
    Changes: Database references
  • Version 1.2: 2024-01-24
    Changes: Data collection, Database references, Derived calculations, Refinement description