Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis

被引：20

作者：

Szurmant, Hendrik ^{[1
]}

Bobay, Benjamin G. ^{[2
]}

White, Robert A. ^{[1
,3
]}

Sullivan, Daniel M. ^{[2
]}

Thompson, Richele J. ^{[2
]}

Hwa, Terence ^{[3
]}

Hoch, James A. ^{[1
]}

Cavanagh, John ^{[2
]}

机构：

[1] Scripps Res Inst, Dept Mol & Expt Med, Div Cellular Biol, La Jolla, CA 92037 USA

[2] N Carolina State Univ, Dept Mol & Struct Biochem, Raleigh, NC 27695 USA

[3] Univ Calif San Diego, Ctr Theoret Biol Phys, San Diego, CA 92037 USA

来源：

BIOCHEMISTRY | 2008年 / 47卷 / 30期

关键词：

D O I：

10.1021/bi8009604

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：

Short-lived protein interactions determine signal transduction specificity among genetically amplified, structurally identical two-component signaling systems. Interacting protein pairs evolve recognition precision by varying residues at specific positions in the,interaction surface consistent with constraints of charge, size, and chemical properties. Such positions can be detected by covariance analyses of two-component protein databases. Here, covariance is shown to identify a cluster of co-evolving dynamic residues in two-component proteins. NMR dynamics and structural studies of both wild-type and mutant proteins in this cluster suggest that motions serve to precisely arrange the site of phosphoryl transfer within the complex.

引用

页码：7782 / 7784

页数：3