6a0f

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Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with Asn-Phe-Ala-Ala-Arg peptideCrystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with Asn-Phe-Ala-Ala-Arg peptide

Structural highlights

6a0f is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NTAN1_HUMAN] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.[1]

References

  1. Cantor JR, Stone EM, Georgiou G. Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. Biochemistry. 2011 Apr 12;50(14):3025-33. doi: 10.1021/bi101832w. Epub 2011 Mar, 18. PMID:21375249 doi:http://dx.doi.org/10.1021/bi101832w

6a0f, resolution 2.38Å

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