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[[Image:1h65.gif|left|200px]]<br />
<applet load="1h65" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1h65, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF PEA TOC34-A NOVEL GTPASE OF THE CHLOROPLAST PROTEIN TRANSLOCON'''<br />


==Overview==
==Crystal structure of pea Toc34 - a novel GTPase of the chloroplast protein translocon==
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.
<StructureSection load='1h65' size='340' side='right'caption='[[1h65]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1h65]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H65 FirstGlance]. <br>
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]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H65 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h65 OCA], [https://pdbe.org/1h65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h65 RCSB], [https://www.ebi.ac.uk/pdbsum/1h65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h65 ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11753431 11753431]
</table>
== Function ==
[https://www.uniprot.org/uniprot/TOC34_PEA TOC34_PEA] GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/1h65_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h65 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
[[Category: Single protein]]
[[Category: Chou CC]]
[[Category: Chou, C.C.]]
[[Category: Forouhar F]]
[[Category: Forouhar, F.]]
[[Category: Hsiao CD]]
[[Category: Hsiao, C.D.]]
[[Category: Kao S]]
[[Category: Kao, S.]]
[[Category: Li HM]]
[[Category: Li, H.M.]]
[[Category: Shr HL]]
[[Category: Shr, H.L.]]
[[Category: Sun YJ]]
[[Category: Sun, Y.J.]]
[[Category: Tu SL]]
[[Category: TU, S.L.]]
[[Category: GDP]]
[[Category: MG]]
[[Category: chloroplast]]
[[Category: gtpase]]
[[Category: translocon]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 13:18:53 2007''

Latest revision as of 14:28, 27 March 2024

Crystal structure of pea Toc34 - a novel GTPase of the chloroplast protein transloconCrystal structure of pea Toc34 - a novel GTPase of the chloroplast protein translocon

Structural highlights

1h65 is a 3 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TOC34_PEA GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1h65, resolution 2.00Å

Drag the structure with the mouse to rotate

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