8WEX

Crystal structure of N-acetyl sugar amidotransferase from Legionella pneumophila

Summary for 8WEX

• Entry DOI: 10.2210/pdb8wex/pdb
• Descriptor: N-acetyl sugar amidotransferase, ZINC ION (3 entities in total)
• Functional Keywords: n-acetyl sugar amidotransferase, rossmanoid fold, pp-loop, lps biosynthesis, transferase
• Biological source: Legionella pneumophila
• Total number of polymer chains: 2
• Total formula weight: 109439.54

Authors

Gao, J.,Xu, W.,Ge, H. (deposition date: 2023-09-19, release date: 2024-05-22)

Primary citation

Gao, J.,Xu, W.,Liu, T.,Sun, W.,Wang, N.,Ma, J.,Ge, H.
Structural Characterization of an N-Acetyl Sugar Amidotransferase Involved in the Lipopolysaccharide Biosynthesis in Bacteria.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: N-acetyl sugar amidotransferase (NASAT) is involved in the lipopolysaccharide (LPS) biosynthesis pathway that catalyzes the formation of the acetamido moiety (sugar-NC(=NH)CH3) on the O-chain. So far, little is known about its structural and functional properties. Here, we report the crystal structure of an N-acetyl sugar amidotransferase from (LpNASAT) at 2.33 Å resolution. LpNASAT folds into a compact basin-shaped architecture with an unusually wide and open putative substrate-binding pocket and a conserved zinc ion-binding tetracysteine motif. The pocket contains a Rossmann-like fold with a PP-loop, suggesting that the NASAT-catalyzed amidotransfer reaction probably requires the conversion of ATP to AMP and PPi. Our data provide structural insights into the NASAT family of proteins, and allow us to possibly identify its functionally important regions.

PubMed: 37895170
DOI: 10.3390/ijms242015491

Experimental method

X-RAY DIFFRACTION (2.33 Å)