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2ihs

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Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide

Structural highlights

2ihs is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUS_DROME Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.^[1] ^[2]

Evolutionary Conservation

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

Publication Abstract from PubMed

B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

Structural basis for protein recognition by B30.2/SPRY domains.,Woo JS, Suh HY, Park SY, Oh BH Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Styhler S, Nakamura A, Lasko P. VASA localization requires the SPRY-domain and SOCS-box containing protein, GUSTAVUS. Dev Cell. 2002 Dec;3(6):865-76. PMID:12479811
↑ Kugler JM, Woo JS, Oh BH, Lasko P. Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors. Mol Cell Biol. 2010 Apr;30(7):1769-82. doi: 10.1128/MCB.01100-09. Epub 2010 Feb, 1. PMID:20123973 doi:http://dx.doi.org/10.1128/MCB.01100-09
↑ Woo JS, Suh HY, Park SY, Oh BH. Structural basis for protein recognition by B30.2/SPRY domains. Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197 doi:10.1016/j.molcel.2006.11.009