Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution.

Literature DB >> 16332443

Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution.

Tim Bergbrede¹, Olena Pylypenko, Alexey Rak, Kirill Alexandrov.

Abstract

Rab/Ypt GTPases represent a>60 member large family of membrane traffic regulators in eukaryotic cells. Members of this group display intrinsic GTPase activity varying over two orders of magnitude. Here, we show that Rab6A represents the RabGTPase with the slowest spontaneous GTPase activity yet measured (5x10(-6)s(-1)). Due to the very low intrinsic hydrolysis rate we were able to crystallise and solve the structure of the Rab6A:GTP complex to 1.82A resolution. Analysis of the structure suggests that low catalytic activity of the Rab6A might be due to high flexibility of the Switch II region and a low degree of constraint of critically important for catalysis Gln 72.

Entities: Chemical Gene

Mesh：

Substances：

Year: 2005 PMID： 16332443 DOI： 10.1016/j.jsb.2005.10.001

Source DB: PubMed Journal: J Struct Biol ISSN： 1047-8477 Impact factor: 2.867

Keyword Cloud
Cited

16 in total

1. Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental, and theoretical IR spectroscopy.

Authors: Till Rudack; Sarah Jenrich; Sven Brucker; Ingrid R Vetter; Klaus Gerwert; Carsten Kötting
Journal: J Biol Chem Date: 2015-08-13 Impact factor: 5.157

2. Protein LidA from Legionella is a Rab GTPase supereffector.

Authors: Stefan Schoebel; Adam L Cichy; Roger S Goody; Aymelt Itzen
Journal: Proc Natl Acad Sci U S A Date: 2011-10-19 Impact factor: 11.205

3. Targeting of the small GTPase Rab6A' by the Legionella pneumophila effector LidA.

Authors: Yang Chen; Matthias P Machner
Journal: Infect Immun Date: 2013-04-08 Impact factor: 3.441

4. Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.

Authors: Kyle P Smith; Pamela J Focia; Srinivas Chakravarthy; Eric C Landahl; Julian L Klosowiak; Sarah E Rice; Douglas M Freymann
Journal: J Struct Biol Date: 2020-10-24 Impact factor: 2.867

5. Catalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail.

Authors: Konstantin Gavriljuk; Emerich-Mihai Gazdag; Aymelt Itzen; Carsten Kötting; Roger S Goody; Klaus Gerwert
Journal: Proc Natl Acad Sci U S A Date: 2012-12-12 Impact factor: 11.205

6. Solution structure of the guanine nucleotide-binding STAS domain of SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis.

Authors: Alok K Sharma; Liwen Ye; Christina E Baer; Kumaran Shanmugasundaram; Tom Alber; Seth L Alper; Alan C Rigby
Journal: J Biol Chem Date: 2010-12-29 Impact factor: 5.157

Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution.

1. Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental, and theoretical IR spectroscopy.

2. Protein LidA from Legionella is a Rab GTPase supereffector.

3. Targeting of the small GTPase Rab6A' by the Legionella pneumophila effector LidA.

4. Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.

5. Catalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail.

6. Solution structure of the guanine nucleotide-binding STAS domain of SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis.

7. A Quantitative Model for BicD2/Cargo Interactions.

8. Crystallization and preliminary X-ray crystallographic studies of Rab6A'(Q72L): a GTP-locked form.

9. Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.

10. Structural and Biophysical Characterization of Rab5a from Leishmania Donovani.