1ltx
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Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid
OverviewOverview
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.
About this StructureAbout this Structure
1LTX is a Protein complex structure of sequences from Rattus norvegicus with ZN, CL and FAR as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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