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1ltx

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Revision as of 08:04, 12 October 2017

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

Structural highlights

1ltx is a 4 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1dce
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [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. [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.

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

Posttranslational geranylgeranylation of Rab GTPases is catalyzed by Rab geranylgeranyltransferase (RabGGTase), which consists of a catalytic alpha/beta heterodimer and an accessory Rab escort protein (REP). The crystal structure of isoprenoid-bound RabGGTase complexed to REP-1 has been solved to 2.7 A resolution. The complex interface buries a surprisingly small surface area of ca. 680 A and is unexpectedly formed by helices 8, 10, and 12 of the RabGGTase alpha subunit and helices D and E of REP-1. We demonstrate that the affinity of RabGGTase for REP-1 is allosterically regulated by phosphoisoprenoid via a long-range trans-domain signal transduction event. Comparing the structure of REP-1 with the closely related RabGDI, we conclude that the specificity of the REP:RabGGTase interaction is defined by differently positioned phenylalanine residues conserved in the REP and GDI subfamilies.

Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase.,Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K Mol Cell. 2003 Feb;11(2):483-94. PMID:12620235^[1]

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

References

↑ Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Mol Cell. 2003 Feb;11(2):483-94. PMID:12620235

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/1ltx"

@@ Line 1: / Line 1: @@
 ==Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid==
 <StructureSection load='1ltx' size='340' side='right' caption='[[1ltx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dce|1dce]]</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=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]</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=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>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1ltx" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Geranylgeranyl transferase|Geranylgeranyl transferase]]
 == References ==
 <references/>

1ltx

From Proteopedia

Revision as of 08:04, 12 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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