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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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Genre: Zeitschriftenartikel
Alternativer Titel : Structure

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 Urheber:
Constantinescu, Alexandru-Tudor1, Autor
Rak, Alexey2, Autor           
Alexandrov, Kirill2, Autor           
Esters, Heike1, Autor
Goody, Roger S.2, Autor           
Scheidig, Axel J.2, Autor           
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

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Schlagwörter: crystal structure; GTP-binding protein; vesicular transport; Ypt7p
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2002-04
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 15557
ISI: 000174863100015
 Art des Abschluß: -

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Titel: Structure
  Alternativer Titel : Structure
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 10 (4) Artikelnummer: - Start- / Endseite: 569 - 579 Identifikator: ISSN: 0969-2126