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Journal Article

Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase

MPS-Authors
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Pylypenko,  Olena
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S1097276503000443/pdfft?md5=19924c026f9cb0e0ab2da1eeaabb6455&pid=1-s2.0-S1097276503000443-main.pdf
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http://dx.doi.org/10.1016/S1097-2765(03)00044-3
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Citation

Pylypenko, O., Rak, A., Reents, R., Niculae, A., Sidorovitch, V., Cioaca, M.-D., et al. (2003). Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Molecular Cell, 11(2), 483-494. doi:10.1016/S1097-2765(03)00044-3.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-0E1A-4
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.