Atomic-resolution crystal structure of the second SH3 domain of yeast Bzz1 determined from a pseudomerohedrally twinned crystalAtomic-resolution crystal structure of the second SH3 domain of yeast Bzz1 determined from a pseudomerohedrally twinned crystal

Structural highlights

2a28 is a 4 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BZZ1_YEAST] Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.[1] [2]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Soulard A, Lechler T, Spiridonov V, Shevchenko A, Shevchenko A, Li R, Winsor B. Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol Cell Biol. 2002 Nov;22(22):7889-906. PMID:12391157
  2. Soulard A, Friant S, Fitterer C, Orange C, Kaneva G, Mirey G, Winsor B. The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis. Protoplasma. 2005 Oct;226(1-2):89-101. Epub 2005 Oct 20. PMID:16231105 doi:http://dx.doi.org/10.1007/s00709-005-0108-4

2a28, resolution 1.07Å

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