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Titolo:
High-resolution crystal structure of S. cerevisiae Ypt51(Delta C15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis
Autore:
Esters, H; Alexandrov, K; Constantinescu, AT; Goody, RS; Scheidig, AJ;
Indirizzi:
Max Planck Inst Mol Physiol, Phys Biochem Abt, D-44227 Dortmund, Germany Max Planck Inst Mol Physiol Dortmund Germany D-44227 7 Dortmund, Germany
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 298, anno: 2000,
pagine: 111 - 121
SICI:
0022-2836(20000421)298:1<111:HCSOSC>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
H-RAS P21; MECHANISM; TRANSPORT; YEAST; HYDROLYSIS; SUBSTRATE; COMPLEX; YPT51P; RAB5;
Keywords:
GTP-binding protein; vesicular transport; crystal structure; Ypt51; Vps21;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Scheidig, AJ Max Planck Inst Mol Physiol, Phys Biochem Abt, Otto Hahn Str 11, D-44227 Dortmund, Germany Max Planck Inst Mol Physiol Otto Hahn Str 11 Dortmund Germany D-44227
Citazione:
H. Esters et al., "High-resolution crystal structure of S. cerevisiae Ypt51(Delta C15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis", J MOL BIOL, 298(1), 2000, pp. 111-121

Abstract

Ypt/Rab proteins are membrane-associated small GTP-binding proteins which play a central role in the coordination, activation and regulation of vesicle-mediated transport in eukaryotic cells. We present the 1.5 Angstrom high-resolution crystal structure of Ypt51 in its active, GppNHp-bound conformation. Ypt51 is an important regulator involved in the endocytic membrane traffic of Saccharomyces cerevisiae. The structure reveals small but significant structural differences compared with H-Ras p21. The effector loop and the catalytic loop are well defined and stabilized by extensive hydrophobic interactions. The switch I and switch II regions form a well-defined epitope for hypothetical effector protein binding. Sequence comparisons between the different isoforms Ypt51, Ypt52 and Ypt53 provide the first insights into determinants for specific effector binding and for fine-tuning of the intrinsic GTP-hydrolysis rate. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 03:12:45