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3cjh

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Tim8-Tim13 complex

Structural highlights

3cjh is a 12 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2bsk
Gene:	TIM13 (ATCC 18824), TIM8 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TIM13_YEAST] Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.^[1] ^[2] ^[3] ^[4] ^[5] [TIM8_YEAST] Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.^[6] ^[7] ^[8] ^[9] ^[10]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Tim8-Tim13 complex, located in the mitochondrial intermembrane space, functions in the TIM22 import pathway that mediates the import of the mitochondrial carriers Tim23, Tim22, and Tim17 into the mitochondrial inner membrane. The Tim8-Tim13 complex assembles as a hexamer and binds to the substrate Tim23 to chaperone the hydrophobic Tim23 across the aqueous intermembrane space. However, both structural features of the Tim8-Tim13 complex and the binding interaction to Tim23 remain poorly defined. The crystal structure of the yeast Tim8-Tim13 complex, reported here at 2.6 A resolution, reveals that the architecture of the Tim8-Tim13 complex is similar to those of other chaperones such as Tim9-Tim10, prefoldin, and Skp, in which long helices extend from a central body like tentacles from a jellyfish. Surface plasmon resonance was applied to investigate interactions between the Tim8-Tim13 complex and Tim23. The Tim8-Tim13 complex contained approximately six binding sites and showed a complex binding interaction indicative of positive cooperativity rather than a simple bimolecular interaction. By combining results from the structural and binding studies, we provide a molecular model of the Tim8-Tim13 complex binding to Tim23. The regions where the tentacle helices attach to the body of the Tim8-Tim13 complex contain six hydrophobic pockets that likely interact with specific sequences of Tim23 and possibly other substrates. Smaller hydrophobic patches on the tentacles themselves likely interact nonspecifically with the substrate's transmembrane helices, shielding it from the aqueous intermembrane space. The central region of Tim23, which enters the intermembrane space first, may serve to nucleate the binding of the Tim8-Tim13 complex, thereby initiating the chaperoned translocation of Tim23 to the mitochondrial inner membrane.

The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23.,Beverly KN, Sawaya MR, Schmid E, Koehler CM J Mol Biol. 2008 Oct 24;382(5):1144-56. Epub 2008 Jul 30. PMID:18706423^[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leuenberger D, Bally NA, Schatz G, Koehler CM. Different import pathways through the mitochondrial intermembrane space for inner membrane proteins. EMBO J. 1999 Sep 1;18(17):4816-22. PMID:10469659 doi:http://dx.doi.org/10.1093/emboj/18.17.4816
↑ Paschen SA, Rothbauer U, Kaldi K, Bauer MF, Neupert W, Brunner M. The role of the TIM8-13 complex in the import of Tim23 into mitochondria. EMBO J. 2000 Dec 1;19(23):6392-400. PMID:11101512 doi:http://dx.doi.org/10.1093/emboj/19.23.6392
↑ Davis AJ, Sepuri NB, Holder J, Johnson AE, Jensen RE. Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria. J Cell Biol. 2000 Sep 18;150(6):1271-82. PMID:10995434
↑ Murphy MP, Leuenberger D, Curran SP, Oppliger W, Koehler CM. The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex. Mol Cell Biol. 2001 Sep;21(18):6132-8. PMID:11509656
↑ Curran SP, Leuenberger D, Schmidt E, Koehler CM. The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. J Cell Biol. 2002 Sep 16;158(6):1017-27. Epub 2002 Sep 9. PMID:12221072 doi:http://dx.doi.org/10.1083/jcb.200205124
↑ Leuenberger D, Bally NA, Schatz G, Koehler CM. Different import pathways through the mitochondrial intermembrane space for inner membrane proteins. EMBO J. 1999 Sep 1;18(17):4816-22. PMID:10469659 doi:http://dx.doi.org/10.1093/emboj/18.17.4816
↑ Paschen SA, Rothbauer U, Kaldi K, Bauer MF, Neupert W, Brunner M. The role of the TIM8-13 complex in the import of Tim23 into mitochondria. EMBO J. 2000 Dec 1;19(23):6392-400. PMID:11101512 doi:http://dx.doi.org/10.1093/emboj/19.23.6392
↑ Davis AJ, Sepuri NB, Holder J, Johnson AE, Jensen RE. Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria. J Cell Biol. 2000 Sep 18;150(6):1271-82. PMID:10995434
↑ Murphy MP, Leuenberger D, Curran SP, Oppliger W, Koehler CM. The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex. Mol Cell Biol. 2001 Sep;21(18):6132-8. PMID:11509656
↑ Curran SP, Leuenberger D, Schmidt E, Koehler CM. The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. J Cell Biol. 2002 Sep 16;158(6):1017-27. Epub 2002 Sep 9. PMID:12221072 doi:http://dx.doi.org/10.1083/jcb.200205124
↑ Beverly KN, Sawaya MR, Schmid E, Koehler CM. The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23. J Mol Biol. 2008 Oct 24;382(5):1144-56. Epub 2008 Jul 30. PMID:18706423 doi:10.1016/j.jmb.2008.07.069

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cjh"

@@ Line 1: / Line 1: @@
 ==Tim8-Tim13 complex==
-<StructureSection load='3cjh' size='340' side='right' caption='[[3cjh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='3cjh' size='340' side='right'caption='[[3cjh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3cjh]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CJH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3cjh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CJH FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bsk|2bsk]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bsk|2bsk]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIM13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), TIM8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIM13 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), TIM8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjh OCA], [http://pdbe.org/3cjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cjh RCSB], [http://www.ebi.ac.uk/pdbsum/3cjh PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjh OCA], [https://pdbe.org/3cjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cjh RCSB], [https://www.ebi.ac.uk/pdbsum/3cjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cjh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TIM13_YEAST TIM13_YEAST]] Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.<ref>PMID:10469659</ref> <ref>PMID:11101512</ref> <ref>PMID:10995434</ref> <ref>PMID:11509656</ref> <ref>PMID:12221072</ref>  [[http://www.uniprot.org/uniprot/TIM8_YEAST TIM8_YEAST]] Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.<ref>PMID:10469659</ref> <ref>PMID:11101512</ref> <ref>PMID:10995434</ref> <ref>PMID:11509656</ref> <ref>PMID:12221072</ref>
+[[https://www.uniprot.org/uniprot/TIM13_YEAST TIM13_YEAST]] Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.<ref>PMID:10469659</ref> <ref>PMID:11101512</ref> <ref>PMID:10995434</ref> <ref>PMID:11509656</ref> <ref>PMID:12221072</ref>  [[https://www.uniprot.org/uniprot/TIM8_YEAST TIM8_YEAST]] Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.<ref>PMID:10469659</ref> <ref>PMID:11101512</ref> <ref>PMID:10995434</ref> <ref>PMID:11509656</ref> <ref>PMID:12221072</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/3cjh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/3cjh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 33: / Line 34: @@
 </StructureSection>
 [[Category: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Beverly, K N]]
 [[Category: Koehler, C M]]

3cjh

From Proteopedia

Current revision

Tim8-Tim13 complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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