3PUY

Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to AMP-PNP after crystal soaking of the pretranslocation state


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.216 

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This is version 2.1 of the entry. See complete history


Literature

Crystal structure of the maltose transporter in a pretranslocation intermediate state.

Oldham, M.L.Chen, J.

(2011) Science 332: 1202-1205

  • DOI: https://doi.org/10.1126/science.1200767
  • Primary Citation of Related Structures:  
    3PUY, 3PUZ, 3PV0

  • PubMed Abstract: 

    Adenosine triphosphate (ATP)-binding cassette (ABC) transporters convert chemical energy from ATP hydrolysis to mechanical work for substrate translocation. They function by alternating between two states, exposing the substrate-binding site to either side of the membrane. A key question that remains to be addressed is how substrates initiate the transport cycle. Using x-ray crystallography, we have captured the maltose transporter in an intermediate step between the inward- and outward-facing states. We show that interactions with substrate-loaded maltose-binding protein in the periplasm induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this conformation then promotes progression to the outward-facing state. These results, interpreted in light of biochemical and functional studies, provide a structural basis to understand allosteric communication in ABC transporters.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, Howard Hughes Medical Institute, West Lafayette, IN 47907, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Maltose transporter subunit; periplasmic-binding component of ABC superfamilyA [auth E]378Escherichia coli K-12Mutation(s): 0 
Gene Names: ECDH10B_4223malE
Membrane Entity: Yes 
UniProt
Find proteins for P0AEX9 (Escherichia coli (strain K12))
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Go to UniProtKB:  P0AEX9
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UniProt GroupP0AEX9
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Maltose transporter subunit; membrane component of ABC superfamilyB [auth F]514Escherichia coli K-12Mutation(s): 0 
Gene Names: ECDH10B_4222malF
Membrane Entity: Yes 
UniProt
Find proteins for P02916 (Escherichia coli (strain K12))
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UniProt GroupP02916
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Maltose transporter subunit; membrane component of ABC superfamilyC [auth G]296Escherichia coli K-12Mutation(s): 0 
Gene Names: ECDH10B_4221malG
Membrane Entity: Yes 
UniProt
Find proteins for P68183 (Escherichia coli (strain K12))
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UniProt GroupP68183
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Fused maltose transport subunit, ATP-binding component of ABC superfamily; regulatory proteinD [auth A],
E [auth B]
381Escherichia coli K-12Mutation(s): 0 
Gene Names: ECDH10B_4224malK
Membrane Entity: Yes 
UniProt
Find proteins for P68187 (Escherichia coli (strain K12))
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Go to UniProtKB:  P68187
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UniProt GroupP68187
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  • Reference Sequence
Oligosaccharides

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Entity ID: 5
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranoseF [auth C]2N/A
Glycosylation Resources
GlyTouCan:  G07411ON
GlyCosmos:  G07411ON
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.216 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.55α = 86.91
b = 96.283β = 80.87
c = 112.283γ = 74.32
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-05-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Structure summary
  • Version 2.1: 2023-09-06
    Changes: Data collection, Database references, Refinement description, Structure summary