Crystal structure of Rab6A '(Q72L) mutant reveals unexpected GDP/Mg2+ binding with opened GTP-binding domain

Title
Crystal structure of Rab6A '(Q72L) mutant reveals unexpected GDP/Mg2+ binding with opened GTP-binding domain
Author(s)
박현호윤종환[윤종환]신영철[신영철]장태호[장태호]김서윤[김서윤]허원도[허원도]서인석[서인석]전주홍[전주홍]
Keywords
TRANS-GOLGI NETWORK; RAB GTPASES; BOUND FORM; PROTEIN; FAMILY; GDP; ORGANIZATION; TRAFFICKING; MECHANISM; MEMBER
Issue Date
201207
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.424, no.2, pp.269 - 273
Abstract
The Ras small G protein-superfamily is a family of GTP hydrolases whose activity is regulated by GTP/GDP binding states. Rab6A, a member of the Ras superfamily, is involved in the regulation of vesicle trafficking, which is critical for endocytosis, biosynthesis, secretion, cell differentiation and cell growth. Rab6A exists in two isoforms, termed RabA and Rab6A'. Substitution of GIn72 to Leu72 (Q72L) at Rab6 family blocks GTP hydrolysis activity and this mutation usually causes the Rab6 protein to be constitutively in an active form. Here, we report the crystal structure of the human Rab6A'(Q72L) mutant form at 1.9 angstrom resolution. Unexpectedly, we found that Rab6AqQ72L) possesses GDP/Mg2+ in the GTP binding pockets, which is formed by a flexible switch I and switch II. Large conformational changes were also detected in the switch I and switch II regions. Our structure revealed that the non-hydrolysable, constitutively active form of Rab6A' can accommodate GDP/Mg2+ in the open conformation. (C) 2012 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/27621http://dx.doi.org/10.1016/j.bbrc.2012.06.102
ISSN
0006-291X
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이과대학 > 화학생화학부 > Articles
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