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PDBsum entry 3w6r
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Signaling protein
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PDB id
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3w6r
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PDB id:
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Signaling protein
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Title:
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Crystal structure of the gap domain of human mgcracgap
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Structure:
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Rac gtpase-activating protein 1. Chain: a. Fragment: rho-gap domain, unp residues 348-546. Synonym: male germ cell racgap, mgcracgap, protein cyk4 homolg, cyk4, hscyk-4. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: racgap1, kiaa1478, mgcracgap. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.90Å
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R-factor:
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0.223
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R-free:
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0.259
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Authors:
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A.Matsuura,H.H.Lee
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Key ref:
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A.Matsuura
and
H.H.Lee
(2013).
Crystal structure of GTPase-activating domain from human MgcRacGAP.
Biochem Biophys Res Commun,
435,
367-372.
PubMed id:
DOI:
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Date:
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21-Feb-13
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Release date:
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26-Feb-14
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PROCHECK
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Headers
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References
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Q9H0H5
(RGAP1_HUMAN) -
Rac GTPase-activating protein 1 from Homo sapiens
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Seq:
Struc:
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632 a.a.
200 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Biochem Biophys Res Commun
435:367-372
(2013)
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PubMed id:
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Crystal structure of GTPase-activating domain from human MgcRacGAP.
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A.Matsuura,
H.H.Lee.
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ABSTRACT
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Cytokinesis in animal cells relies on a centralspindlin complex consisting of
male germ cell RacGap (MgcRacGAP) and mitotic kinesin-like protein 1 (MKLP1).
Rho GTPases act as molecular switches to regulate the actin cytoskeleton for
cytokinesis, of which Rac1 is regulated by MgcRacGAP. In this study, we
determined the crystal structure of the GTPase-activating protein (GAP) domain
of MgcRacGAP at a resolution of 1.9Å. The conformation of Arg385, which is a
key residue for GAP activity, was found to be different from that of previously
reported GAP proteins, and MgcRacGAP (residues 348-546) was found to exist as a
monomer in solution, according to Stokes radii. We also measured the GAP
activity of MgcRacGAP mutants for Rac1.
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Links
