2ihs

Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptideCrystal 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.
Related:	2fnj, 2fbe
Gene:	gus (Drosophila melanogaster)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[VASA_DROME] Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

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^[9]

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

References

↑ Lasko PF, Ashburner M. The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A. Nature. 1988 Oct 13;335(6191):611-7. PMID:3140040 doi:http://dx.doi.org/10.1038/335611a0
↑ Hay B, Jan LY, Jan YN. A protein component of Drosophila polar granules is encoded by vasa and has extensive sequence similarity to ATP-dependent helicases. Cell. 1988 Nov 18;55(4):577-87. PMID:3052853
↑ Liang L, Diehl-Jones W, Lasko P. Localization of vasa protein to the Drosophila pole plasm is independent of its RNA-binding and helicase activities. Development. 1994 May;120(5):1201-11. PMID:8026330
↑ Styhler S, Nakamura A, Swan A, Suter B, Lasko P. vasa is required for GURKEN accumulation in the oocyte, and is involved in oocyte differentiation and germline cyst development. Development. 1998 May;125(9):1569-78. PMID:9521895
↑ Carrera P, Johnstone O, Nakamura A, Casanova J, Jackle H, Lasko P. VASA mediates translation through interaction with a Drosophila yIF2 homolog. Mol Cell. 2000 Jan;5(1):181-7. PMID:10678180
↑ 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
↑ Liu N, Dansereau DA, Lasko P. Fat facets interacts with vasa in the Drosophila pole plasm and protects it from degradation. Curr Biol. 2003 Oct 28;13(21):1905-9. PMID:14588248
↑ Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell. 2006 Apr 21;125(2):287-300. PMID:16630817 doi:10.1016/j.cell.2006.01.054
↑ 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

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OCA

[1] Lasko PF, Ashburner M. The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A. Nature. 1988 Oct 13;335(6191):611-7. PMID:3140040 doi:http://dx.doi.org/10.1038/335611a0

[2] Hay B, Jan LY, Jan YN. A protein component of Drosophila polar granules is encoded by vasa and has extensive sequence similarity to ATP-dependent helicases. Cell. 1988 Nov 18;55(4):577-87. PMID:3052853

[3] Liang L, Diehl-Jones W, Lasko P. Localization of vasa protein to the Drosophila pole plasm is independent of its RNA-binding and helicase activities. Development. 1994 May;120(5):1201-11. PMID:8026330

[4] Styhler S, Nakamura A, Swan A, Suter B, Lasko P. vasa is required for GURKEN accumulation in the oocyte, and is involved in oocyte differentiation and germline cyst development. Development. 1998 May;125(9):1569-78. PMID:9521895

[5] Carrera P, Johnstone O, Nakamura A, Casanova J, Jackle H, Lasko P. VASA mediates translation through interaction with a Drosophila yIF2 homolog. Mol Cell. 2000 Jan;5(1):181-7. PMID:10678180

[6] 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

[7] Liu N, Dansereau DA, Lasko P. Fat facets interacts with vasa in the Drosophila pole plasm and protects it from degradation. Curr Biol. 2003 Oct 28;13(21):1905-9. PMID:14588248

[8] Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell. 2006 Apr 21;125(2):287-300. PMID:16630817 doi:10.1016/j.cell.2006.01.054

[9] 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

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