1dpf
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(New page: 200px<br /> <applet load="1dpf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dpf, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:28, 12 November 2007
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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 with GDP as ligand. 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
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