1LTX

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

Summary for 1LTX

• Entry DOI: 10.2210/pdb1ltx/pdb
• Related: 1DCE
• Descriptor: RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT, RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT, Rab Escort Protein 1, ... (8 entities in total)
• Functional Keywords: rab prenylation, prenyltransferase, lucine-rich repeats, post-translational modification, transferase-protein binding complex, transferase/protein binding
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm, cytosol : P37727
• Total number of polymer chains: 4
• Total formula weight: 175077.09

Authors

Pylypenko, O.,Rak, A.,Reents, R.,Niculae, A.,Thoma, N.H.,Waldmann, H.,Schlichting, I.,Goody, R.S.,Alexandrov, K. (deposition date: 2002-05-21, release date: 2003-05-21, Last modification date: 2023-10-25)

Primary citation

Pylypenko, O.,Rak, A.,Reents, R.,Niculae, A.,Sidorovitch, V.,Cioaca, M.D.,Bessolitsyna, E.,Thoma, N.H.,Waldmann, H.,Schlichting, I.,Goody, R.S.,Alexandrov, K.
Structure of Rab Escort Protein-1 in Complex with Rab Geranylgeranyltransferase
Mol.Cell, 11:483-494, 2003

PubMed Abstract: 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.

PubMed: 12620235
DOI: 10.1016/S1097-2765(03)00044-3

Experimental method

X-RAY DIFFRACTION (2.7 Å)