Versatile modes of peptide recognition by the AAA plus adaptor protein SspB

被引：35

作者：

Levchenko, I

Grant, RA

Flynn, JM

Sauer, RT

Baker, TA

机构：

[1] MIT, Dept Biol, Cambridge, MA 02139 USA

[2] Howard Hughes Med Inst, Cambridge, MA 02139 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 06期

关键词：

D O I：

10.1038/nsmb934

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：

Energy-dependent proteases often rely on adaptor proteins to modulate substrate recognition. The SspB adaptor binds peptide sequences in the stress-response regulator RseA and in ssrA-tagged proteins and delivers these molecules to the AAA+ ClpXP protease for degradation. The structure of SspB bound to an ssrA peptide is known. Here, we report the crystal structure of a complex between SspB and its recognition peptide in RseA. Notably, the RseA sequence is positioned in the peptide-binding groove of SspB in a direction opposite to the ssrA peptide, the two peptides share only one common interaction with the adaptor, and the RseA interaction site is substantially larger than the overlapping ssrA site. This marked diversity in SspB recognition of different target proteins indicates that it is capable of highly flexible and dynamic substrate delivery.

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页码：520 / 525

页数：6

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