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Title: Crystal structure of inactive form of Rab3B

Abstract

Rab proteins are the largest family of ras-related GTPases in eukaryotic cells. They act as directional molecular switches at membrane trafficking, including vesicle budding, cargo sorting, transport, tethering, and fusion. Here, we generated and crystallized the Rab3B:GDP complex. The structure of the complex was solved to 1.9 {angstrom} resolution and the structural base comparison with other Rab3 members provides a structural basis for the GDP/GTP switch in controlling the activity of small GTPase. The comparison of charge distribution among the members of Rab3 also indicates their different roles in vesicular trafficking.

Authors:
; ; ; ; ;  [1];  [2];  [2]
  1. (Hebei)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
FOREIGNINDUSTRY
OSTI Identifier:
1038293
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochem. Biophys. Res. Commun.; Journal Volume: 418; Journal Issue: (4) ; 02, 2012
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CARGO; CHARGE DISTRIBUTION; CRYSTAL STRUCTURE; GTP-ASES; MEMBRANES; PROTEINS; RESOLUTION; SORTING; SWITCHES; TRANSPORT

Citation Formats

Zhang, Wei, Shen, Yang, Jiao, Ronghong, Liu, Yanli, Deng, Lingfu, Qi, Chao, Toronto), and Huazhong). Crystal structure of inactive form of Rab3B. United States: N. p., 2012. Web. doi:10.1016/j.bbrc.2012.01.124.
Zhang, Wei, Shen, Yang, Jiao, Ronghong, Liu, Yanli, Deng, Lingfu, Qi, Chao, Toronto), & Huazhong). Crystal structure of inactive form of Rab3B. United States. doi:10.1016/j.bbrc.2012.01.124.
Zhang, Wei, Shen, Yang, Jiao, Ronghong, Liu, Yanli, Deng, Lingfu, Qi, Chao, Toronto), and Huazhong). Thu . "Crystal structure of inactive form of Rab3B". United States. doi:10.1016/j.bbrc.2012.01.124.
@article{osti_1038293,
title = {Crystal structure of inactive form of Rab3B},
author = {Zhang, Wei and Shen, Yang and Jiao, Ronghong and Liu, Yanli and Deng, Lingfu and Qi, Chao and Toronto) and Huazhong)},
abstractNote = {Rab proteins are the largest family of ras-related GTPases in eukaryotic cells. They act as directional molecular switches at membrane trafficking, including vesicle budding, cargo sorting, transport, tethering, and fusion. Here, we generated and crystallized the Rab3B:GDP complex. The structure of the complex was solved to 1.9 {angstrom} resolution and the structural base comparison with other Rab3 members provides a structural basis for the GDP/GTP switch in controlling the activity of small GTPase. The comparison of charge distribution among the members of Rab3 also indicates their different roles in vesicular trafficking.},
doi = {10.1016/j.bbrc.2012.01.124},
journal = {Biochem. Biophys. Res. Commun.},
number = (4) ; 02, 2012,
volume = 418,
place = {United States},
year = {Thu Jun 28 00:00:00 EDT 2012},
month = {Thu Jun 28 00:00:00 EDT 2012}
}
  • Highlights: Black-Right-Pointing-Pointer This is the first structural information of human Rab3B. Black-Right-Pointing-Pointer To provides a structural basis for the GDP/GTP switch in controlling the activity of Rab3. Black-Right-Pointing-Pointer The charge distribution of Rab3B indicates its unique roles in vesicular trafficking. -- Abstract: Rab proteins are the largest family of ras-related GTPases in eukaryotic cells. They act as directional molecular switches at membrane trafficking, including vesicle budding, cargo sorting, transport, tethering, and fusion. Here, we generated and crystallized the Rab3B:GDP complex. The structure of the complex was solved to 1.9 A resolution and the structural base comparison with other Rab3 membersmore » provides a structural basis for the GDP/GTP switch in controlling the activity of small GTPase. The comparison of charge distribution among the members of Rab3 also indicates their different roles in vesicular trafficking.« less
  • The R-diastereomer of phosphorothioate analogs of cGMP, Rp-cGMPS, is one of few known inhibitors of cGMP-dependent protein kinase I (PKG I); however, its mechanism of inhibition is currently not fully understood. We determined the crystal structure of the PKG Iβ cyclic nucleotide-binding domain (PKG Iβ CNB-B), considered a ‘gatekeeper’ for cGMP activation, bound to Rp-cGMPS at 1.3 Å. Our structural and NMR data show that PKG Iβ CNB-B bound to Rp-cGMPS displays an apo-like structure with its helical domain in an open conformation. Comparison with the cAMP-dependent protein kinase regulatory subunit (PKA RIα) showed that this conformation resembles the catalyticmore » subunit-bound inhibited state of PKA RIα more closely than the apo or Rp-cAMPS-bound conformations. Our results suggest that Rp-cGMPS inhibits PKG I by stabilizing the inactive conformation of CNB-B.« less
  • The reaction of the paramagnetic Rh/sub 2//sup 5+/ complex Rh/sub 2/(form)/sub 3/(NO/sub 3/)/sub 2/ (form = N,N'-di-p-tolylformamidinate) with an excess of the neutral ligands PPh/sub 3/, pyridine, and dimethylamine leads, via reductive elimination of one nitrate group, to the formation of the asymmetric Rh/sub 2//sup 4+/ complexes Rh/sub 2/(form)/sub 3/(NO/sub 3/)L L = PPh/sub 3/ (1), pyridine (2), N(CH/sub 3/)/sub 2/H (3). The two rhodium atoms in complexes 1-3 display different coordinations and reduced average formal oxidation states. The complexes have been characterized by IR, /sup 31/P NMR, and /sup 103/Rh NMR spectroscopic methods, which point out the nonequivalence ofmore » the two rhodium atoms. Complexes 1 and 2 have also been characterized by single-crystal X-ray analysis. Complex 1 belongs to the monoclinic space group system P2/sub 1//n, with a = 21.529 (3) /angstrom/; b = 23.990 (3) /angstrom/, c = 11.944 (1) /angstrom/, /beta/ = 102.13 (4)/degree/, Z = 4, and R = 0.057 for 2046 reflections with I > 3/sigma/(I). The crystal structure reveals that one of the three formamidinate groups spanning the dimetal center (Rh-Rh = 2.498 (2) /angstrom/) is bonded in an unusual way, namely, /sigma/,/sigma/-N,N' with a localized double bond. Complex 2 forms monoclinic crystals in space group P2/sub 1//c with a = 10.238 (1) /angstrom/, b = 16.567 (2) /angstrom/, /beta/ = 955.6 (3)/degree/, Z = 4, and R = 0.041 for 3392 reflections with I > 3/sigma/(I). In complexes 2 and 3 of all the bridging ligands are bonded in the usual fashion, namely, /sigma/,/sigma/-N,N' with delocalized double bonds. 18 refs., 3 figs., 6 tabs..« less