3BC1

Crystal Structure of the complex Rab27a-Slp2a

Summary for 3BC1

• Entry DOI: 10.2210/pdb3bc1/pdb
• Related: 2iey 2iez 2if0
• Descriptor: Ras-related protein Rab-27A, Synaptotagmin-like protein 2, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• Functional Keywords: rab27, gtpase, rab, signaling protein, gdpnp, slp2a, exophilin-4, gtp-binding, lipoprotein, membrane, methylation, nucleotide-binding, prenylation, signaling protein-transport protein complex, signaling protein/transport protein
• Biological source: Mus musculus (Mouse); More
• Cellular location: Membrane; Lipid-anchor: Q9ERI2; Isoform 1: Cytoplasm. Isoform 4: Cell membrane: Q9HCH5
• Total number of polymer chains: 4
• Total formula weight: 59540.90

Authors

Chavas, L.M.G.,Ihara, K.,Kawasaki, M.,Wakatsuki, S. (deposition date: 2007-11-12, release date: 2008-09-02, Last modification date: 2023-11-01)

Primary citation

Chavas, L.M.G.,Ihara, K.,Kawasaki, M.,Torii, S.,Uejima, T.,Kato, R.,Izumi, T.,Wakatsuki, S.
Elucidation of Rab27 recruitment by its effectors: structure of Rab27a bound to Exophilin4/Slp2-a
Structure, 16:1468-1477, 2008

PubMed Abstract: Rab GTPases coordinate vesicular trafficking within eukaryotic cells by collaborating with a set of effector proteins. Rab27a regulates numerous exocytotic pathways, and its dysfunction causes the Griscelli syndrome human immunodeficiency. Exophilin4/Slp2-a localizes on phosphatidylserine-enriched plasma membrane, and its N-terminal Rab27-binding domain (RBD27) specifically recognizes Rab27 on the surfaces of melanosomes and secretory granules prior to docking and fusion. To characterize the selective binding of Rab27 to 11 various effectors, we have determined the 1.8 A resolution structure of Rab27a in complex with Exophilin4 RBD27. The effector packs against the switch and interswitch elements of Rab27a, and specific affinity toward Rab27a is modulated by a shift in the orientation of the effector structural motif (S/T)(G/L)xW(F/Y)(2). The observed structural complementation between the interacting surfaces of Rab27a and Exophilin4 sheds light on the disparities among the Rab27 effectors and outlines a general mechanism for their recruitment.

PubMed: 18940603
DOI: 10.1016/j.str.2008.07.015

Experimental method

X-RAY DIFFRACTION (1.8 Å)