SASDEF2: Mitochondrial import inner membrane translocase complex TIM9·10

Basic information

• Entry: Database: SASBDB / ID: SASDEF2

Sample

Mitochondrial import inner membrane translocase complex TIM9·10

• Mitochondrial import inner membrane translocase subunit TIM9 (protein), TIM9, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
• Mitochondrial import inner membrane translocase subunit TIM10 (protein), Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Function / homology

Function:

mitochondrial intermembrane space chaperone complex / Mitochondrial protein import / TIM22 mitochondrial import inner membrane insertion complex / protein transporter activity / protein insertion into mitochondrial inner membrane / mitochondrial intermembrane space / unfolded protein binding / mitochondrial inner membrane / mitochondrion / metal ion binding

Domain/homology:

: / Tim10-like / Tim10-like domain superfamily / Tim10/DDP family zinc finger

Component:

Mitochondrial import inner membrane translocase subunit TIM9 / Mitochondrial import inner membrane translocase subunit TIM10

• Biological species: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Citation: Journal: Cell / Year: 2018; Title: Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.; Authors: Katharina Weinhäupl / Caroline Lindau / Audrey Hessel / Yong Wang / Conny Schütze / Tobias Jores / Laura Melchionda / Birgit Schönfisch / Hubert Kalbacher / Beate Bersch / Doron Rapaport / Martha Brennich / Kresten Lindorff-Larsen / Nils Wiedemann / Paul Schanda / ; Abstract: The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial "transfer-chaperone" system is able to guide α-helical and β-barrel membrane proteins in a "nascent chain-like" conformation through a ribosome-free compartment.

Contact author

• Martha Brennich (EMBL, European Molecular Biology Laboratory (EMBL) - Grenoble Outstation, Grenoble, France)

Models

• Model #2188: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.57; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2189: ; Type: dummy / Software: (r6669) / Radius of dummy atoms: 2.10 A / Symmetry: C3 / Chi-square value: 1.378; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2236: ; Type: atomic; Comment: The model is a snapshot from the ensemble creating the fit.; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Mitochondrial import inner membrane translocase complex TIM9·10; Specimen concentration: 1.00-5.00 / Entity id: 1218 / 1219
• Buffer: Name: 50mM Tris, 150mM NaCl / pH: 7.4

Entity #1218

Name: TIM9 / Type: protein
Description: Mitochondrial import inner membrane translocase subunit TIM9
Formula weight: 10.202 / Num. of mol.: 3
Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
References: UniProt: O74700
Sequence:

MDALNSKEQQ EFQKVVEQKQ MKDFMRLYSN LVERCFTDCV NDFTTSKLTN KEQTCIMKCS EKFLKHSERV GQRFQEQNAA LGQGLGR

Entity #1219

Type: protein
Description: Mitochondrial import inner membrane translocase subunit TIM10
Formula weight: 10.23 / Num. of mol.: 3
Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
References: UniProt: P87108
Sequence:

GSFLGFGGGQ PQLSSQQKIQ AAEAELDLVT DMFNKLVNNC YKKCINTSYS EGELNKNESS CLDRCVAKYF ETNVQVGENM QKMGQSFNAA GKF

Experimental information

• Beam: Instrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.099 Å / Dist. spec. to detc.: 2.864 mm
• Detector: Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm

Scan

Title: Mitochondrial import inner membrane translocase complex TIM9·10
Measurement date: Aug 27, 2015 / Storage temperature: 35 °C / Cell temperature: 20 °C / Exposure time: 20 sec. / Number of frames: 1 / Unit: 1/nm /

	Min	Max
Q	0.0599	4.9389

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 687 /

	Min	Max
Q	0.121051	3.34866
P(R) point	1	687
R	0	10

Result

Type of curve: merged

	Experimental	Standard	Standard error	Porod
MW	61 kDa	49.97 kDa	10	61 kDa
Volume	-	-	-	103 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	50.28	49.97	0.03
Radius of gyration, Rg	2.725 nm	2.67 nm	0.01

	Min	Max
D	-	10
Guinier point	7	91