An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+.

Abstract:

:Mg2+ is essential for guanosine triphosphatase activity and plays key roles in guanine nucleotide binding and preserving the structural integrity of GTP-binding proteins. To understand the structural basis for Mg2+ function during the GDP/GTP exchange process, we determined the crystal structure of Delta9-Sar1-GDP at low Mg2+ concentration at 1.8A. Two Sar1-GDP molecules in the crystal form a dimer with Mg2+ presenting only in molecule B but not in molecule A. The absence of Mg2+ induces significant conformational changes in the switch I region in molecule A that shows similarities with those of Ha-Ras bound to Sos. The current structure reveals an important regulatory role for Mg2+. We suggest that guanine nucleotide exchange factor may utilize this feature to generate an open conformation for GDP/GTP exchange. Furthermore, we propose a mechanism for COPII assembly and disassembly in which dimerization of Sar1 plays an important role.

authors

Rao Y,Bian C,Yuan C,Li Y,Chen L,Ye X,Huang Z,Huang M

doi

10.1016/j.bbrc.2006.07.148

subject

Has Abstract

pub_date

2006-09-29 00:00:00

pages

908-15

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01662-7

journal_volume

348

pub_type

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