Protein Family Models

Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane [1]. Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region [1]. This family includes the C-terminal region of Tim44 that has been shown to form a stable proteolytic fragment in yeast. This region is also found in a set of smaller bacterial proteins. The molecular function of the bacterial members of this family is unknown but transport seems likely. The crystal structure of the C terminal of Tim44 has revealed a large hydrophobic pocket which might play an important role in interacting with the acyl chains of lipid molecules in the mitochondrial membrane [3]. [1]. 10430866. Domain structure and lipid interaction of recombinant yeast Tim44. Weiss C, Oppliger W, Vergeres G, Demel R, Jeno P, Horst M, de Kruijff B, Schatz G, Azem A;. Proc Natl Acad Sci U S A 1999;96:8890-8894. [2]. 16511294. Preliminary crystallographic studies of yeast mitochondrial peripheral membrane protein Tim44p. Josyula R, Jin Z, McCombs D, DeLucas L, Sha B;. Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006;62:172-174. [3]. 16647716. Crystal structure of yeast mitochondrial peripheral membrane protein Tim44p C-terminal domain. Josyula R, Jin Z, Fu Z, Sha B;. J Mol Biol. 2006;359:798-804. (from Pfam)

Date:

2024-10-16

Tim44 domain-containing protein similar to mitochondrial 39S ribosomal protein L45 and to mitochondrial import inner membrane translocase subunit Tim44, an essential component of the eukaryotic PAM complex which is required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner

Date:

2019-05-20