This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1h65

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:58, 10 January 2018

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

Structural highlights

1h65 is a 3 chain structure with sequence from Garden pea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
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.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sun YJ, Forouhar F, Li Hm HM, Tu SL, Yeh YH, Kao S, Shr HL, Chou CC, Chen C, Hsiao CD. Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein translocon. Nat Struct Biol. 2002 Feb;9(2):95-100. PMID:11753431 doi:10.1038/nsb744

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h65"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF PEA TOC34 - A NOVEL GTPASE OF THE CHLOROPLAST PROTEIN TRANSLOCON==
+==Crystal structure of pea Toc34 - a novel GTPase of the chloroplast protein translocon==
 <StructureSection load='1h65' size='340' side='right' caption='[[1h65]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h65 OCA], [http://pdbe.org/1h65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h65 RCSB], [http://www.ebi.ac.uk/pdbsum/1h65 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h65 OCA], [http://pdbe.org/1h65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h65 RCSB], [http://www.ebi.ac.uk/pdbsum/1h65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h65 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/1h65_consurf.spt"</scriptWhenChecked>
+    <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>

1h65

From Proteopedia

Revision as of 08:58, 10 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox