Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase

Rak, Alexey, Reents, Reinhard, Pylypenko, Olena, Niculae, Anca, Sidorovitch, Vadim, Thoma, Nicolas H., Waldmann, Herbert, Schlichting, Ilme, Goody, Roger S. and Alexandrov,Kirill (2001) Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Journal of Structural Biology, 136 2: 158-161. doi:10.1006/jsbi.2001.4433


Author Rak, Alexey
Reents, Reinhard
Pylypenko, Olena
Niculae, Anca
Sidorovitch, Vadim
Thoma, Nicolas H.
Waldmann, Herbert
Schlichting, Ilme
Goody, Roger S.
Alexandrov,Kirill
Title Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase
Journal name Journal of Structural Biology   Check publisher's open access policy
ISSN 1047-8477
1095-8657
Publication date 2001-11
Sub-type Article (original research)
DOI 10.1006/jsbi.2001.4433
Open Access Status Not yet assessed
Volume 136
Issue 2
Start page 158
End page 161
Total pages 4
Place of publication Maryland Heights, MO, United States
Publisher Academic Press
Language eng
Formatted abstract
Posttranslational prenylation of proteins is a widespread phenomenon and the majority of prenylated proteins are geranylgeranylated members of the Rab GTPase family. Geranylgeranylation is catalyzed by Rab geranylgeranyltransferase (RabGGTase) and is critical for the ability of Rab protein to mediate vesicular docking and fusion of various intracellular vesicles. RabGGTase consists of a catalytic α/β heterodimer and an accessory protein termed Rab escort protein (REP-1) that delivers the newly prenylated Rab proteins to their target membrane. Mutations in the REP-1 gene in humans lead to an X-chromosome-linked defect known as choroideremia - a debilitating disease that inevitably culminates in complete blindness. Here we report in vitro assembly and purification of the stoichiometric ternary complex of RabGGTase with REP-1 stabilized by a hydrolysis-resistant phosphoisoprenoid analog - farnesyl phosphonyl(methyl)phoshonate. The complex formed crystals of extended plate morphology under low ionic-strength conditions. X-ray diffraction data were collected to 2.8 Å resolution at the ESRF. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 68.7, b = 197.7, c = 86.1 Å, β = 113.4°. Preliminary structural analysis revealed the presence of one molecule in the asymmetric unit.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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