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- SASDEG2: Mitochondrial import inner membrane translocase complex TIM9·10 i... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDEG2 |
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![]() | Mitochondrial import inner membrane translocase complex TIM9·10 in complex with a precursor (GDP/GTP carrier (Ggc1))
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Function / homology | ![]() guanine nucleotide transport / mitochondrial intermembrane space protein transporter complex / Mitochondrial protein import / TIM22 mitochondrial import inner membrane insertion complex / guanine nucleotide transmembrane transporter activity / protein insertion into mitochondrial inner membrane / protein transporter activity / mitochondrial genome maintenance / mitochondrial intermembrane space / transmembrane transport ...guanine nucleotide transport / mitochondrial intermembrane space protein transporter complex / Mitochondrial protein import / TIM22 mitochondrial import inner membrane insertion complex / guanine nucleotide transmembrane transporter activity / protein insertion into mitochondrial inner membrane / protein transporter activity / mitochondrial genome maintenance / mitochondrial intermembrane space / transmembrane transport / unfolded protein binding / intracellular iron ion homeostasis / membrane => GO:0016020 / mitochondrial inner membrane / mitochondrion / metal ion binding Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() 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 ...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 ...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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Models
Model #2193 | ![]() Type: dummy / Software: (r5575) / Radius of dummy atoms: 3.40 A / Symmetry: C1 / Chi-square value: 1.358 / P-value: 0.000045 ![]() |
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Model #2224 | ![]() Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 1.89 ![]() |
Model #2237 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2238 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2239 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2240 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2241 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2242 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2243 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
Model #2244 | ![]() Type: atomic Comment: Snapshot from a 7ns coarse-grained simulation. Fit corresponds to weighte ensemble, based on 16 runs ![]() |
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Sample
![]() | Name: Mitochondrial import inner membrane translocase complex TIM9·10 in complex with a precursor (GDP/GTP carrier (Ggc1)) Specimen concentration: 2 mg/ml / Entity id: 1215 / 1216 / 1217 |
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Buffer | Name: 50mM Tris, 150mM NaCl, imidiazole / pH: 7.4 Comment: The imidiazole concentration varies between 200 mM and 300 mM |
Entity #1215 | Name: TIM9 / Type: protein Description: Mitochondrial import inner membrane translocase subunit TIM9 Formula weight: 10.202 / Num. of mol.: 6 Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) References: UniProt: O74700 Sequence: MDALNSKEQQ EFQKVVEQKQ MKDFMRLYSN LVERCFTDCV NDFTTSKLTN KEQTCIMKCS EKFLKHSERV GQRFQEQNAA LGQGLGR |
Entity #1216 | Name: TIM10 / Type: protein Description: Mitochondrial import inner membrane translocase subunit TIM10 Formula weight: 10.23 / Num. of mol.: 6 Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) References: UniProt: P87108 Sequence: GSFLGFGGGQ PQLSSQQKIQ AAEAELDLVT DMFNKLVNNC YKKCINTSYS EGELNKNESS CLDRCVAKYF ETNVQVGENM QKMGQSFNAA GKF |
Entity #1217 | Name: GGC1 / Type: protein / Description: Mitochondrial GTP/GDP carrier protein 1 / Formula weight: 33.426 / Num. of mol.: 1 Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) References: UniProt: P38988 Sequence: QSGLARLLGS ASAGIMEIAV FHPVDTISKR LMSNHTKITS GQELNRVIFR DHFSEPLGKR LFTLFPGLGY AASYKVLQRV YKYGGQPFAN EFLNKHYKKD FDNLFGEKTG KAMRSAAAGS LIGIGEIVLL PLDVLKIKRQ TNPESFKGRG FIKILRDEGL FNLYRGWGWT ...Sequence: QSGLARLLGS ASAGIMEIAV FHPVDTISKR LMSNHTKITS GQELNRVIFR DHFSEPLGKR LFTLFPGLGY AASYKVLQRV YKYGGQPFAN EFLNKHYKKD FDNLFGEKTG KAMRSAAAGS LIGIGEIVLL PLDVLKIKRQ TNPESFKGRG FIKILRDEGL FNLYRGWGWT AARNAPGSFA LFGGNAFAKE YILGLKDYSQ ATWSQNFISS IVGASSSLIV SAPLDVIKTR IQNRNFDNPE SGLRIVKNTL KNEGVTAFFK GLTPKLLTTG PKLVFSFALA QSLIPRFDNL LSKLEHHHHH H |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Feb 22, 2016 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 50 / Unit: 1/nm /
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Distance distribution function P(R) |
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Result |
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