6UKS

ATPgammaS bound mBcs1


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein.

Tang, W.K.Borgnia, M.J.Hsu, A.L.Esser, L.Fox, T.de Val, N.Xia, D.

(2020) Nat Struct Mol Biol 27: 202-209

  • DOI: https://doi.org/10.1038/s41594-020-0373-0
  • Primary Citation of Related Structures:  
    6U1Y, 6UKO, 6UKP, 6UKS

  • PubMed Abstract: 

    The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory Complex III. How Bcs1 translocates ISP across the membrane is unknown. Here we report structures of mouse Bcs1 in two different conformations, representing three nucleotide states. The apo and ADP-bound structures reveal a homo-heptamer and show a large putative substrate-binding cavity accessible to the matrix space. ATP binding drives a contraction of the cavity by concerted motion of the ATPase domains, which could push substrate across the membrane. Our findings shed light on the potential mechanism of translocating folded proteins across a membrane, offer insights into the assembly process of Complex III and allow mapping of human disease-associated mutations onto the Bcs1 structure.


  • Organizational Affiliation

    Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial chaperone BCS1
A, B, C, D, E
A, B, C, D, E, F, G
427Mus musculusMutation(s): 0 
Gene Names: Bcs1l
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q9CZP5 (Mus musculus)
Explore Q9CZP5 
Go to UniProtKB:  Q9CZP5
IMPC:  MGI:1914071
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9CZP5
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
AGS (Subject of Investigation/LOI)
Query on AGS

Download Ideal Coordinates CCD File 
I [auth A]
J [auth B]
L [auth C]
N [auth D]
P [auth E]
I [auth A],
J [auth B],
L [auth C],
N [auth D],
P [auth E],
R [auth F],
T [auth G]
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
C10 H16 N5 O12 P3 S
NLTUCYMLOPLUHL-KQYNXXCUSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
H [auth A]
K [auth B]
M [auth C]
O [auth D]
Q [auth E]
H [auth A],
K [auth B],
M [auth C],
O [auth D],
Q [auth E],
S [auth F],
U [auth G]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Cancer Institute (NIH/NCI)United States--

Revision History  (Full details and data files)

  • Version 1.0: 2020-02-05
    Type: Initial release
  • Version 1.1: 2020-02-12
    Changes: Database references
  • Version 1.2: 2020-02-26
    Changes: Database references