5nkz

Crystal structure of H. polymorpha ubiquitin conjugating enzyme Pex4p in complex with soluble domain of Pex22p

spinqualitylabelsall models 5nkz, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nkz is a 4 chain structure with sequence from Ogataea angusta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UBCX_PICAN Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5.[PROSITE-ProRule:PRU00388] Publication Abstract from PubMed Pex4p is a peroxisomal E2 involved in ubiquitinating the conserved cysteine residue of the cycling receptor protein Pex5p. Previously, we demonstrated that Pex4p from the yeast Saccharomyces cerevisiae binds directly to the peroxisomal membrane protein Pex22p and that this interaction is vital for receptor ubiquitination. In addition, Pex22p binding allows Pex4p to specifically produce lysine 48 linked ubiquitin chains in vitro through an unknown mechanism. This activity is likely to play a role in targeting peroxisomal proteins for proteasomal degradation. Here we present the crystal structures of Pex4p alone and in complex with Pex22p from the yeast Hansenula polymorpha. Comparison of the two structures demonstrates significant differences to the active site of Pex4p upon Pex22p binding while molecular dynamics simulations suggest that Pex22p binding facilitates active site remodelling of Pex4p through an allosteric mechanism. Taken together, our data provide insights into how Pex22p binding allows Pex4p to build K48-linked Ub chains. Structural insights into K48-linked ubiquitin chain formation by the Pex4p-Pex22p complex.,Groves MR, Schroer CFE, Middleton AJ, Lunev S, Danda N, Ali AM, Marrink SJ, Williams C Biochem Biophys Res Commun. 2017 Dec 28. pii: S0006-291X(17)32552-4. doi:, 10.1016/j.bbrc.2017.12.150. PMID:29288668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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