1EK0

GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION

Summary for 1EK0

• Entry DOI: 10.2210/pdb1ek0/pdb
• Descriptor: PROTEIN (GTP-BINDING PROTEIN YPT51), MAGNESIUM ION, NICKEL (II) ION, ... (6 entities in total)
• Functional Keywords: g protein, vesicular traffic, gtp hydrolysis, ypt/rab protein, endocytosis, hydrolase, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endosome membrane ; Lipid- anchor : P36017
• Total number of polymer chains: 1
• Total formula weight: 20012.06

Authors

Esters, H.,Scheidig, A.J. (deposition date: 2000-03-06, release date: 2000-04-17, Last modification date: 2024-10-09)

Primary citation

Esters, H.,Alexandrov, K.,Constantinescu, A.T.,Goody, R.S.,Scheidig, A.J.
High-resolution crystal structure of S. cerevisiae Ypt51(DeltaC15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis.
J.Mol.Biol., 298:111-121, 2000

PubMed 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 A 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.

PubMed: 10756108
DOI: 10.1006/jmbi.2000.3645

Experimental method

X-RAY DIFFRACTION (1.48 Å)