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2guz

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Revision as of 23:33, 24 December 2014

Structure of the Tim14-Tim16 complex of the mitochondrial protein import motor

Structural highlights

2guz is a 16 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1xbl, 1hdj
Gene:	PAM18, TIM14 (Saccharomyces cerevisiae), PAM16, TIM16 (Saccharomyces cerevisiae)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TIM14_YEAST] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).^[1] ^[2] ^[3] [TIM16_YEAST] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.^[4] ^[5] ^[6]

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 import motor of the mitochondrial translocase of the inner membrane (TIM23) mediates the ATP-dependent translocation of preproteins into the mitochondrial matrix by cycles of binding to and release from mtHsp70. An essential step of this process is the stimulation of the ATPase activity of mtHsp70 performed by the J cochaperone Tim14. Tim14 forms a complex with the J-like protein Tim16. The crystal structure of this complex shows that the conserved domains of the two proteins have virtually identical folds but completely different surfaces enabling them to perform different functions. The Tim14-Tim16 dimer reveals a previously undescribed arrangement of J and J-like domains. Mutations that destroy the complex between Tim14 and Tim16 are lethal demonstrating that complex formation is an essential requirement for the viability of cells. We further demonstrate tight regulation of the cochaperone activity of Tim14 by Tim16. The first crystal structure of a J domain in complex with a regulatory protein provides new insights into the function of the mitochondrial TIM23 translocase and the Hsp70 chaperone system in general.

Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor.,Mokranjac D, Bourenkov G, Hell K, Neupert W, Groll M EMBO J. 2006 Oct 4;25(19):4675-85. Epub 2006 Sep 14. PMID:16977310^[7]

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

References

↑ Mokranjac D, Sichting M, Neupert W, Hell K. Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. EMBO J. 2003 Oct 1;22(19):4945-56. PMID:14517234 doi:http://dx.doi.org/10.1093/emboj/cdg485
↑ Truscott KN, Voos W, Frazier AE, Lind M, Li Y, Geissler A, Dudek J, Muller H, Sickmann A, Meyer HE, Meisinger C, Guiard B, Rehling P, Pfanner N. A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria. J Cell Biol. 2003 Nov 24;163(4):707-13. PMID:14638855 doi:http://dx.doi.org/10.1083/jcb.200308004
↑ D'Silva PD, Schilke B, Walter W, Andrew A, Craig EA. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13839-44. Epub 2003 Nov 6. PMID:14605210 doi:http://dx.doi.org/10.1073/pnas.1936150100
↑ Li Y, Dudek J, Guiard B, Pfanner N, Rehling P, Voos W. The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18. J Biol Chem. 2004 Sep 3;279(36):38047-54. Epub 2004 Jun 24. PMID:15218029 doi:http://dx.doi.org/10.1074/jbc.M404319200
↑ Frazier AE, Dudek J, Guiard B, Voos W, Li Y, Lind M, Meisinger C, Geissler A, Sickmann A, Meyer HE, Bilanchone V, Cumsky MG, Truscott KN, Pfanner N, Rehling P. Pam16 has an essential role in the mitochondrial protein import motor. Nat Struct Mol Biol. 2004 Mar;11(3):226-33. Epub 2004 Feb 15. PMID:14981507 doi:http://dx.doi.org/10.1038/nsmb735
↑ Kozany C, Mokranjac D, Sichting M, Neupert W, Hell K. The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase. Nat Struct Mol Biol. 2004 Mar;11(3):234-41. Epub 2004 Feb 15. PMID:14981506 doi:http://dx.doi.org/10.1038/nsmb734
↑ Mokranjac D, Bourenkov G, Hell K, Neupert W, Groll M. Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor. EMBO J. 2006 Oct 4;25(19):4675-85. Epub 2006 Sep 14. PMID:16977310

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/2guz"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2guz]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GUZ FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xbl|1xbl]], [[1hdj|1hdj]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xbl|1xbl]], [[1hdj|1hdj]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAM18, TIM14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), PAM16, TIM16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAM18, TIM14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), PAM16, TIM16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2guz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2guz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2guz RCSB], [http://www.ebi.ac.uk/pdbsum/2guz PDBsum]</span></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=2guz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2guz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2guz RCSB], [http://www.ebi.ac.uk/pdbsum/2guz PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TIM14_YEAST TIM14_YEAST]] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).<ref>PMID:14517234</ref> <ref>PMID:14638855</ref> <ref>PMID:14605210</ref>  [[http://www.uniprot.org/uniprot/TIM16_YEAST TIM16_YEAST]] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.<ref>PMID:15218029</ref> <ref>PMID:14981507</ref> <ref>PMID:14981506</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Bourenkov, G.]]
+[[Category: Bourenkov, G]]
-[[Category: Groll, M.]]
+[[Category: Groll, M]]
-[[Category: Hell, K.]]
+[[Category: Hell, K]]
-[[Category: Mokranjac, D.]]
+[[Category: Mokranjac, D]]
-[[Category: Neupert, W.]]
+[[Category: Neupert, W]]
 [[Category: Chaperone]]
 [[Category: Dnaj-fold]]
 [[Category: Protein transport]]

2guz

From Proteopedia

Revision as of 23:33, 24 December 2014

Structure of the Tim14-Tim16 complex of the mitochondrial protein import motor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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