1h65: Difference between revisions
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[[Image:1h65.gif|left|200px]]<br /><applet load="1h65" size=" | [[Image:1h65.gif|left|200px]]<br /><applet load="1h65" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1h65, resolution 2.0Å" /> | caption="1h65, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF PEA TOC34-A NOVEL GTPASE OF THE CHLOROPLAST PROTEIN TRANSLOCON'''<br /> | '''CRYSTAL STRUCTURE OF PEA TOC34-A NOVEL GTPASE OF THE CHLOROPLAST PROTEIN TRANSLOCON'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1H65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain C'>AC1</scene>. Full crystallographic information is available from [http:// | 1H65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H65 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: translocon]] | [[Category: translocon]] | ||
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Revision as of 10:46, 3 February 2008
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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 species whose, GTPase activity is significantly reduced compared to that of wild type, Toc34. These results, together with a number of structural features unique, to Toc34, suggest that each monomer acts as a GAP on the other interacting, monomer.
About this StructureAbout this Structure
1H65 is a Single protein structure of sequence from Pisum sativum with and as ligands. Known structural/functional Site: . 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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