2o6v

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spinqualitylabelsall models 2o6v, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH

Overview

Ubiquitin modification of proteins is used as a signal in many cellular, processes. Lysine side-chains can be modified by a single ubiquitin or by, a polyubiquitin chain, which is defined by an isopeptide bond between the, C terminus of one ubiquitin and a specific lysine in a neighboring, ubiquitin. Polyubiquitin conformations that result from different lysine, linkages presumably differentiate their roles and ability to bind specific, targets and enzymes. However, conflicting results have been obtained, regarding the precise conformation of Lys48-linked tetraubiquitin. We, report the crystal structure of Lys48-linked tetraubiquitin at, near-neutral pH. The two tetraubiquitin complexes in the asymmetric unit, show the complete connectivity of the chain and the molecular details of, the interactions. This tetraubiquitin conformation is consistent with our, NMR data as well as with previous studies of diubiquitin and, tetraubiquitin in solution at neutral pH. The structure provides a basis, for understanding Lys48-linked polyubiquitin recognition under, physiological conditions.

About this Structure

2O6V is a Protein complex structure of sequences from Homo sapiens with SO4 and MES as ligands. Full crystallographic information is available from OCA.

Reference

Crystal Structure and Solution NMR Studies of Lys48-linked Tetraubiquitin at Neutral pH., Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C, J Mol Biol. 2007 Mar 16;367(1):204-11. Epub 2006 Dec 29. PMID:17240395

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