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.
Copyright 2000 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Crystallography, X-Ray
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Endocytosis*
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Enzyme Activation
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Guanylyl Imidodiphosphate / metabolism*
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Hydrogen Bonding
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Hydrolysis
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Magnesium / metabolism
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Models, Molecular
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Molecular Sequence Data
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Nickel / metabolism
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Structure, Tertiary
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Proto-Oncogene Proteins p21(ras) / chemistry
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Rats
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Saccharomyces cerevisiae / chemistry*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Sequence Alignment
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Sequence Deletion
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Structure-Activity Relationship
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rab GTP-Binding Proteins / chemistry*
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rab GTP-Binding Proteins / genetics
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rab GTP-Binding Proteins / metabolism*
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rab3A GTP-Binding Protein / chemistry
Substances
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Protein Isoforms
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Saccharomyces cerevisiae Proteins
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Guanylyl Imidodiphosphate
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Nickel
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VPS21 protein, S cerevisiae
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Proto-Oncogene Proteins p21(ras)
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rab GTP-Binding Proteins
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rab3A GTP-Binding Protein
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Magnesium