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1ltx

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<StructureSection load='1ltx' size='340' side='right'caption='[[1ltx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1ltx' size='340' side='right'caption='[[1ltx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ltx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LTX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ltx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAR:FARNESYL'>FAR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dce|1dce]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAR:FARNESYL'>FAR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=1ltx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltx OCA], [http://pdbe.org/1ltx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ltx RCSB], [http://www.ebi.ac.uk/pdbsum/1ltx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ltx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltx OCA], [https://pdbe.org/1ltx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltx RCSB], [https://www.ebi.ac.uk/pdbsum/1ltx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PGTA_RAT PGTA_RAT]] Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively. [[http://www.uniprot.org/uniprot/RAE1_RAT RAE1_RAT]] Binds unprenylated Rab proteins, presents it to the catalytic Rab GGTase dimer, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Also a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation. [[http://www.uniprot.org/uniprot/PGTB2_RAT PGTB2_RAT]] Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively.
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[https://www.uniprot.org/uniprot/PGTA_RAT PGTA_RAT] Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alexandrov, K]]
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[[Category: Rattus norvegicus]]
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[[Category: Goody, R S]]
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[[Category: Alexandrov K]]
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[[Category: Niculae, A]]
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[[Category: Goody RS]]
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[[Category: Pylypenko, O]]
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[[Category: Niculae A]]
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[[Category: Rak, A]]
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[[Category: Pylypenko O]]
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[[Category: Reents, R]]
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[[Category: Rak A]]
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[[Category: Schlichting, I]]
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[[Category: Reents R]]
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[[Category: Thoma, N H]]
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[[Category: Schlichting I]]
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[[Category: Waldmann, H]]
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[[Category: Thoma NH]]
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[[Category: Lucine-rich repeat]]
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[[Category: Waldmann H]]
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[[Category: Post-translational modification]]
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[[Category: Prenyltransferase]]
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[[Category: Rab prenylation]]
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[[Category: Transferase-protein binding complex]]
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Current revision

Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid

PDB ID 1ltx

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