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  Rab-Subfamily-Specific Regions of Ypt7p Are Structurally Different from Other RabGTPases

Constantinescu, A.-T., Rak, A., Alexandrov, K., Esters, H., Goody, R. S., & Scheidig, A. J. (2002). Rab-Subfamily-Specific Regions of Ypt7p Are Structurally Different from Other RabGTPases. Structure, 10(4), 569-579.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-0E9F-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-0EA0-4
Genre: Journal Article
Alternative Title : Structure

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 Creators:
Constantinescu, Alexandru-Tudor1, Author
Rak, Alexey2, Author              
Alexandrov, Kirill2, Author              
Esters, Heike1, Author
Goody, Roger S.2, Author              
Scheidig, Axel J.2, Author              
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, escidoc:1753286              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, escidoc:1753289              

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Free keywords: crystal structure; GTP-binding protein; vesicular transport; Ypt7p
 Abstract: The GTPase Ypt7p from S. cerevisiae is involved in late endosome-to-vacuole transport and homotypic vacuole fusion. We present crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p solved at 1.35 and 1.6 Angstrom resolution, respectively. Despite the similarity of the overall structure to other Ypt/Rab proteins, Ypt7p displays small but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37 cause a difference in the main chain trace of the RabSF2 region and form a characteristic surface epitope, Ypt7p(.)GppNHp does not display the helix alpha2, characteristic of the Ras-superfamily, but instead possess an extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring RabSF1 and RabSF4 regions are different in their conformations to those of other Ypt/Rab proteins.

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Language(s): eng - English
 Dates: 2002-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 15557
ISI: 000174863100015
 Degree: -

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Title: Structure
  Alternative Title : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 10 (4) Sequence Number: - Start / End Page: 569 - 579 Identifier: ISSN: 0969-2126