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University of Groningen Structural and biochemical characterization of Roco proteins Terheyden, Susanne

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University of Groningen

Structural and biochemical characterization of Roco proteins

Terheyden, Susanne

IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from

it. Please check the document version below.

Document Version

Publisher's PDF, also known as Version of record

Publication date:

2018

Link to publication in University of Groningen/UMCG research database

Citation for published version (APA):

Terheyden, S. (2018). Structural and biochemical characterization of Roco proteins. University of

Groningen.

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Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum.

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Chapter 2

Revisiting the Roco G-protein cycle

Susanne Terheyden*, Franz Y. Ho*, Bernd K. Gilsbach*, Alfred Wittinghofer and Arjan

Kortholt

*equal contribution

This chapter has been published in:

Biochem. J. 2015,

465, 139–147.

ST and BG performed all biochemical and structural experiments with the bacterial proteins

and FH with human LRRK2. AW and AK designed the experiments and all authors

contributed to the writing of the paper.

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Supplementary Information

Figure S1. Sequence alignment. Homo sapiens (Hs) LRRK2 (Swiss: Q5S007), Chlorobium

tepidum (Ct) Roco (Swiss: Q8KC98) and Methanosarcina barkeri (Mb) Roco2 (Swiss:

Q46A62) sequences were aligned using the PRALINE sequence alignment server [1] and

GeneDoc (http://www.psc.edu/biomed/genedoc). Black and grey background represents the

sequence identity in three or two sequences, respectively. Structural elements of the

G-domain (lines), construct boundaries (horizontal arrows), and important residues (vertical

arrows) are indicated above the alignment.

1 Simossis, V. A. and Heringa, J. (2005) PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information. Nucleic Acids Res. 33, W289–94.

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