metadata
license: mit
language:
- en
tags:
- biology
- protein structure
- token classification
widget:
- text: >-
N-terminal acetylation (Nt-acetylation), carried out by N-terminal
acetyltransferases (NATs), is a conserved and primary modification of
nascent peptide chains. Naa60 (also named NatF) is a recently identified
NAT found only in multicellular eukaryotes. This protein was shown to
locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of
transmembrane proteins, and it also harbors lysine Nε-acetyltransferase
(KAT) activity to catalyze the acetylation of lysine ε-amine. Here, we
report the crystal structures of human Naa60 (hNaa60) in complex with
Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA). The hNaa60 protein
contains an amphipathic helix following its GNAT domain that may
contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted
different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal
structures. Remarkably, we found that the side-chain of Phe 34 can
influence the position of the coenzyme, indicating a new regulatory
mechanism involving enzyme, co-factor and substrates interactions.
Moreover, structural comparison and biochemical studies indicated that Tyr
97 and His 138 are key residues for catalytic reaction and that a
non-conserved β3-β4 long loop participates in the regulation of hNaa60
activity.
model-index:
- name: BiomedNLP-PubMedBERT-ProteinStructure-NER-v2.1
results:
- task:
name: NER
type: token-classification
metrics:
- name: NER Precision
type: precision
value: null
- name: NER Recall
type: recall
value: null
- name: NER F Score
type: f_score
value: null