5NNP

Structure of Naa15/Naa10 bound to HypK-THB

Summary for 5NNP

• Entry DOI: 10.2210/pdb5nnp/pdb
• Descriptor: N-terminal acetyltransferase-like protein, Putative uncharacterized protein, Ser-Glu-Ser-Ser, ... (8 entities in total)
• Functional Keywords: n-acetylation, nats, naa15, naa10, hypk, nata, nat1, ard1, bisubstrate analogue, transferase
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); More
• Total number of polymer chains: 8
• Total formula weight: 233229.53

Authors

Weyer, F.A.,Gumiero, A.,Kopp, J.,Sinning, I. (deposition date: 2017-04-10, release date: 2017-06-14, Last modification date: 2024-11-13)

Primary citation

Weyer, F.A.,Gumiero, A.,Lapouge, K.,Bange, G.,Kopp, J.,Sinning, I.
Structural basis of HypK regulating N-terminal acetylation by the NatA complex.
Nat Commun, 8:15726-15726, 2017

PubMed Abstract: 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.

PubMed: 28585574
DOI: 10.1038/ncomms15726

Experimental method

X-RAY DIFFRACTION (2.602 Å)