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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Rao Y,Bian C,Yuan C,Li Y,Chen L,Ye X,Huang Z,Huang Mdoi
10.1016/j.bbrc.2006.07.148subject
Has Abstractpub_date
2006-09-29 00:00:00pages
908-15issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(06)01662-7journal_volume
348pub_type
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