1h65: Difference between revisions
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Revision as of 16:25, 30 October 2007
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CRYSTAL STRUCTURE OF PEA TOC34-A NOVEL GTPASE OF THE CHLOROPLAST PROTEIN TRANSLOCON
OverviewOverview
Toc34, a 34-kDa integral membrane protein, is a member of the Toc, (translocon at the outer-envelope membrane of chloroplasts) complex, which, associates with precursor proteins during protein transport across the, chloroplast outer membrane. Here we report the 2.0 A resolution crystal, structure of the cytosolic part of pea Toc34 in complex with GDP and Mg2+., In the crystal, Toc34 molecules exist as dimers with features resembling, those found in a small GTPase in complex with a GTPase activating protein, (GAP). However, gel filtration experiments revealed that dimeric and, monomeric forms of Toc34 coexisted in phosphate saline buffer solution at, pH 7.2. Mutation of Arg 128, an essential residue for dimerization, to an, Ala residue led to the formation of an exclusively monomeric ... [(full description)]
About this StructureAbout this Structure
1H65 is a [Single protein] structure of sequence from [Pisum sativum] with MG and GDP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein translocon., Sun YJ, Forouhar F, Li Hm HM, Tu SL, Yeh YH, Kao S, Shr HL, Chou CC, Chen C, Hsiao CD, Nat Struct Biol. 2002 Feb;9(2):95-100. PMID:11753431
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