1iym
From Proteopedia
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RING-H2 finger domain of EL5
Overview
EL5, a RING-H2 finger protein, is rapidly induced by, N-acetylchitooligosaccharides in rice cell. We expressed the EL5 RING-H2, finger domain in Escherichia coli and determined its structure in solution, by NMR spectroscopy. The EL5 RING-H2 finger domain consists of, two-stranded beta-sheets (beta1, Ala(147)-Phe(149); beta2, Gly(156)-His(158)), one alpha-helix (Cys(161)-Leu(166)), and two large N-, and C-terminal loops. It is stabilized by two tetrahedrally coordinated, zinc ions. This structure is similar to that of other RING finger domains, of proteins of known function. From structural analogies, we inferred that, the EL5 RING-H2 finger is a binding domain for ubiquitin-conjugating, enzyme (E2). The binding site is probably formed by solvent-exposed, hydrophobic residues of the N- and C-terminal loops and the alpha-helix., We demonstrated that the fusion protein with EL5-(96-181) and, maltose-binding protein (MBP) was polyubiquitinated by incubation with, ubiquitin, ubiquitin-activating enzyme (E1), and a rice E2 protein, OsUBC5b. This supported the idea that the EL5 RING finger domain is, essential for ubiquitin-ligase activity of EL5. By NMR titration, experiments, we identified residues that are critical for the interaction, between the EL5 RING-H2 finger and OsUBC5b. We conclude that the RING-H2, finger domain of EL5 is the E2 binding site of EL5.
About this Structure
1IYM is a Single protein structure of sequence from Oryza sativa with ZN as ligand. Full crystallographic information is available from OCA.
Reference
High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice protein whose expression is increased upon exposure to pathogen-derived oligosaccharides., Katoh S, Hong C, Tsunoda Y, Murata K, Takai R, Minami E, Yamazaki T, Katoh E, J Biol Chem. 2003 Apr 25;278(17):15341-8. Epub 2003 Feb 14. PMID:12588869
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