5nnp

Structure of Naa15/Naa10 bound to HypK-THB

spinqualitylabelsall models 5nnp, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nnp is a 8 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.602Å Ligands: CMC, FME, GOL, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0S4M4_CHATD Publication Abstract from PubMed In eukaryotes, N-terminal acetylation is one of the most common protein modifications involved in a wide range of biological processes. Most N-acetyltransferase complexes (NATs) act co-translationally, with the heterodimeric NatA complex modifying the majority of substrate proteins. Here we show that the Huntingtin yeast two-hybrid protein K (HypK) binds tightly to the NatA complex comprising the auxiliary subunit Naa15 and the catalytic subunit Naa10. The crystal structures of NatA bound to HypK or to a N-terminal deletion variant of HypK were determined without or with a bi-substrate analogue, respectively. The HypK C-terminal region is responsible for high-affinity interaction with the C-terminal part of Naa15. In combination with acetylation assays, the HypK N-terminal region is identified as a negative regulator of the NatA acetylation activity. Our study provides mechanistic insights into the regulation of this pivotal protein modification. Structural basis of HypK regulating N-terminal acetylation by the NatA complex.,Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I Nat Commun. 2017 Jun 6;8:15726. doi: 10.1038/ncomms15726. PMID:28585574 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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