2fif

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spinqualitylabelsall models 2fif, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin

Overview

Rabex-5 is an exchange factor for Rab5, a master regulator of endosomal, trafficking. Rabex-5 binds monoubiquitin, undergoes covalent, ubiquitination and contains an intrinsic ubiquitin ligase activity, all of, which require an N-terminal A20 zinc finger followed immediately by a, helix. The structure of the N-terminal portion of Rabex-5 bound to, ubiquitin at 2.5-A resolution shows that Rabex-5-ubiquitin interactions, occur at two sites. The first site is a new type of ubiquitin-binding, domain, an inverted ubiquitin-interacting motif, which binds with, approximately 29-microM affinity to the canonical Ile44 hydrophobic patch, on ubiquitin. The second is a diaromatic patch on the A20 zinc finger, which binds with approximately 22-microM affinity to a polar region, centered on Asp58 of ubiquitin. The A20 zinc-finger diaromatic patch, mediates ubiquitin-ligase activity by directly recruiting a, ubiquitin-loaded ubiquitin-conjugating enzyme.

About this Structure

2FIF is a Protein complex structure of sequences from Bos taurus with ZN and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5., Lee S, Tsai YC, Mattera R, Smith WJ, Kostelansky MS, Weissman AM, Bonifacino JS, Hurley JH, Nat Struct Mol Biol. 2006 Mar;13(3):264-71. Epub 2006 Feb 5. PMID:16462746

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