Abstract
The Rnd proteins constitute an exceptional subfamily within the Rho GTPase family. They possess extended chains at both termini and four prominent amino acid deviations causing GTPase deficiency. Herein, we report the crystal structure of the Rnd3/RhoE G-domain (amino acids 19-200) at 2.0 A resolution. This is the first GTP-structure of a Rho family member which reveals a similar fold but striking differences from RhoA concerning (i) GTPase center, (ii) charge distribution at several surface areas, (iii) C3-transferase binding site and (iv) interacting interfaces towards RhoA regulators and effectors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ADP Ribose Transferases / chemistry
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Binding Sites / physiology
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Botulinum Toxins*
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Crystallography, X-Ray
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GTPase-Activating Proteins / chemistry*
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Guanine Nucleotide Dissociation Inhibitors / chemistry
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Guanine Nucleotide Exchange Factors / chemistry
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Guanosine Triphosphate / chemistry
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Humans
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Models, Molecular*
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Molecular Sequence Data
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Protein Binding / physiology
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Protein Structure, Tertiary / physiology
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Rho Guanine Nucleotide Exchange Factors
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
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rho GTP-Binding Proteins
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rho-Specific Guanine Nucleotide Dissociation Inhibitors
Substances
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GTPase-Activating Proteins
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Guanine Nucleotide Dissociation Inhibitors
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Guanine Nucleotide Exchange Factors
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Rho Guanine Nucleotide Exchange Factors
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rho GTPase-activating protein
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rho-Specific Guanine Nucleotide Dissociation Inhibitors
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Guanosine Triphosphate
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ADP Ribose Transferases
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exoenzyme C3, Clostridium botulinum
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Botulinum Toxins
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RND3 protein, human
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rho GTP-Binding Proteins