3LGE

Crystal structure of rabbit muscle aldolase-SNX9 LC4 complex

Summary for 3LGE

• Entry DOI: 10.2210/pdb3lge/pdb
• Descriptor: Fructose-bisphosphate aldolase A, Sorting nexin-9 (3 entities in total)
• Functional Keywords: complex, glycolysis, actin dynamics, lc4, hydrophobic pocket, acetylation, lyase, phosphoprotein, schiff base, protein transport, sh3 domain, transport, lyase-protein binding complex, lyase/protein binding
• Biological source: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits); More
• Total number of polymer chains: 8
• Total formula weight: 171112.52

Authors

Rangarajan, E.S.,Park, H.,Fortin, E.,Sygusch, J.,Izard, T. (deposition date: 2010-01-20, release date: 2010-02-02, Last modification date: 2023-09-06)

Primary citation

Rangarajan, E.S.,Park, H.,Fortin, E.,Sygusch, J.,Izard, T.
Mechanism of aldolase control of sorting nexin 9 function in endocytosis.
J.Biol.Chem., 285:11983-11990, 2010

PubMed Abstract: Sorting nexin 9 (SNX9) functions in a complex with the GTPase dynamin-2 at clathrin-coated pits, where it provokes fission of vesicles to complete endocytosis. Here the SNX9.dynamin-2 complex binds to clathrin and adapter protein complex 2 (AP-2) that line these pits, and this occurs through interactions of the low complexity domain (LC4) of SNX9 with AP-2. Intriguingly, localization of the SNX9.dynamin-2 complex to clathrin-coated pits is blocked by interactions with the abundant glycolytic enzyme aldolase, which also binds to the LC4 domain of SNX9. The crystal structure of the LC4 motif of human SNX9 in complex with aldolase explains the biochemistry and biology of this interaction, where SNX9 binds near the active site of aldolase via residues 165-171 that are also required for the interactions of SNX9 with AP-2. Accordingly, SNX9 binding to aldolase is structurally precluded by the binding of substrate to the active site. Interactions of SNX9 with aldolase are far more extensive and differ from those of the actin-nucleating factor WASP with aldolase, indicating considerable plasticity in mechanisms that direct the functions of the aldolase as a scaffold protein.

PubMed: 20129922
DOI: 10.1074/jbc.M109.092049

Experimental method

X-RAY DIFFRACTION (2.2 Å)