Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
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DOI:
10.1038/nsmb.2636
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发表时间:
2013-09
影响因子:
16.8
通讯作者:
Marmorstein R
中科院分区:
文献类型:
--
作者:
Liszczak G;Goldberg JM;Foyn H;Petersson EJ;Arnesen T;Marmorstein R
Amino-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this co-translational modification, the heterodimeric NatA complex harbors the most diversity for substrate selection and modifies the majority of all amino-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100 kDa holo-NatA complex from Schizosaccharomyces pombe in the absence and presence of a bisubstrate peptide-CoA conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 TPR motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases.
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
DOI:
10.1107/s0907444909052925
发表时间:
2010-02
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
作者:
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者:
Zwart PH
影响因子:
4.8
作者:
Liszczak, Glen;Arnesen, Thomas;Marmorstein, Ronen
通讯作者:
Marmorstein, Ronen
影响因子:
9.8
作者:
Forte GM;Pool MR;Stirling CJ
通讯作者:
Stirling CJ
影响因子:
4.8
作者:
Evjenth, Rune;Hole, Kristine;Lillehaug, Johan R.
通讯作者:
Lillehaug, Johan R.