9FTC

Aeromonas caviae CMP-Pse5Ac7Ac synthetase in the presence of CMP-Pse5Ac7Ac.

This is a non-PDB format compatible entry.

Summary for 9FTC

• Entry DOI: 10.2210/pdb9ftc/pdb
• Descriptor: NeuA, (2~{R},4~{S},5~{S},6~{S})-5-acetamido-6-[(1~{S},2~{S})-1-acetamido-2-oxidanyl-propyl]-2-[[(2~{R},3~{S},4~{R},5~{R})-5-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-4-oxidanyl-oxane-2-carboxylic acid (3 entities in total)
• Functional Keywords: carbohydrate synthesis, pseudaminic acid synthesis, cmp-transferase, transferase
• Biological source: Aeromonas caviae
• Total number of polymer chains: 2
• Total formula weight: 57302.69

Authors

Cowan, A.R.,Hemsworth, G.R.,Keenan, T.,Fascione, M.A. (deposition date: 2024-06-24, release date: 2024-10-09, Last modification date: 2024-12-18)

Primary citation

Keenan, T.,Cowan, A.R.,Flack, E.K.P.,Hatton, N.E.,Walklett, A.J.,Thomas, G.H.,Hemsworth, G.R.,Fascione, M.A.
Structural dissection of the CMP-pseudaminic acid synthetase, PseF.
Structure, 32:2399-, 2024

PubMed Abstract: Pseudaminic acid is a non-mammalian sugar found in the surface glycoconjugates of many bacteria, including several human pathogens, and is a virulence factor thought to facilitate immune evasion. The final step in the biosynthesis of the nucleotide activated form of the sugar, CMP-Pse5Ac7Ac is performed by a CMP-Pse5Ac7Ac synthetase (PseF). Here we present the biochemical and structural characterization of PseF from Aeromonas caviae (AcPseF), with AcPseF displaying metal-dependent activity over a broad pH and temperature range. Upon binding to CMP-Pse5Ac7Ac, AcPseF undergoes dynamic movements akin to other CMP-ulosonic acid synthetases. The enzyme clearly discriminates Pse5Ac7Ac from other ulosonic acids, through active site interactions with side-chain functional groups and by positioning the molecule in a hydrophobic pocket. Finally, we show that AcPseF binds the CMP-Pse5Ac7Ac side chain in the lowest energy conformation, a trend that we observed in the structures of other enzymes of this class.

PubMed: 39393361
DOI: 10.1016/j.str.2024.09.017

Experimental method

X-RAY DIFFRACTION (1.5 Å)