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1dpf
From Proteopedia
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| , resolution 2.0Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP
Overview
Mg(2+) ions are essential for guanosine triphosphatase (GTPase) activity and play key roles in guanine nucleotide binding and preserving the structural integrity of GTP-binding proteins. We determined the crystal structure of a small GTPase RHOA complexed with GDP in the absence of Mg(2+) at 2.0-A resolution. Elimination of a Mg(2+) ion induces significant conformational changes in the switch I region that opens up the nucleotide-binding site. Similar structural changes have been observed in the switch regions of Ha-Ras bound to its guanine nucleotide exchange factor, Sos. This RHOA-GDP structure reveals an important regulatory role for Mg(2+) and suggests that guanine nucleotide exchange factor may utilize this feature of switch I to produce an open conformation in GDP/GTP exchange.
About this Structure
1DPF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism., Shimizu T, Ihara K, Maesaki R, Kuroda S, Kaibuchi K, Hakoshima T, J Biol Chem. 2000 Jun 16;275(24):18311-7. PMID:10748207
Page seeded by OCA on Thu Mar 20 10:42:08 2008
