2e2z
From Proteopedia
Solution NMR structure of yeast Tim15, co-chaperone of mitochondrial Hsp70
Structural highlights
FunctionZIM17_YEAST Involved in protein import into mitochondria. Acts as a Hsp70-specific chaperone that prevents self-aggregation of the matrix Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their function in mitochondrial protein import and Fe/S protein biosynthesis. May act together with PAM18 as co-chaperone to facilitate recognition and folding of imported proteins by SSC1 in the mitochondrial matrix.[1] [2] [3] [4] 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 PubMedMitochondrial heat-shock protein 70 (mtHsp70) and its partner proteins drive protein import into the matrix. Tim15/Zim17/Hep1 is a mtHsp70 partner protein on the matrix side of the inner mitochondrial membrane. We determined the nuclear magnetic resonance (NMR) structure of the core domain of Tim15. On the basis of the NMR structure, we created Tim15 mutants and tested their ability to complement the functional defects of Tim15 depletion and to suppress self-aggregation of mtHsp70 in vivo. A pair of basic residues, Arg 106 and His 107, conserved Asp 111 and flexible loop 133-137, and were important (Arg 106-His 107 pair and Asp 111) or partly important (the loop 133-137) for yeast cell growth, mitochondrial protein import and the suppression of mtHsp70 aggregation. Therefore, the function of Tim15 in yeast cell growth is well correlated with its ability to suppress mtHsp70 aggregation, although it is still unknown whether inhibition of mtHsp70 aggregation is the primary function of Tim15. Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70.,Momose T, Ohshima C, Maeda M, Endo T EMBO Rep. 2007 Jul;8(7):664-70. Epub 2007 Jun 15. PMID:17571076[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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