The α-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family

被引:18
作者
Zhang, H
Grishin, NV [1 ]
机构
[1] Natl Lib Med, Natl Ctr Biotechnol Informat, NIH, Bethesda, MD 20894 USA
[2] Univ Maryland, Inst Biotechnol, Rockville, MD 20850 USA
[3] Ctr Adv Res Biotechnol, Rockville, MD 20850 USA
关键词
helix packing; protein evolution; protein-protein interactions; protein prenyltransferases; tetratricopeptide repeat;
D O I
10.1110/ps.8.8.1658
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lipidation catalyzed by protein prenyltransferases is essential for the biological function of a number of eukaryotic proteins, many of which are involved in signal transduction and vesicular traffic regulation. Sequence similarity searches reveal that the alpha-subunit of protein prenyltransferases (PT alpha) is a member of the tetratricopeptide repeat (TPR) superfamily. This finding makes the three-dimensional structure of the rat protein farnesyltransferase the first structural model of a TPR protein interacting with its protein partner. Structural comparison of the two TPR domains in protein farnesyltransferase and protein phosphatase 5 indicates that variation in TPR consensus residues may affect protein binding specificity through altering the overall shape of the TPR superhelix. A general approach to evolutionary analysis of proteins with repetitive sequence motifs has been developed and applied to the protein prenyltransferases and other TPR proteins. The results suggest that all members in PT alpha family originated from a common multirepeat ancestor, while the common ancestor of PT alpha and other members of TPR superfamily is likely to be a single repeat protein.
引用
收藏
页码:1658 / 1667
页数:10
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