9FTB
Aeromonas caviae CMP-Pse5A7Ac Synthetase
Summary for 9FTB
| Entry DOI | 10.2210/pdb9ftb/pdb |
| Descriptor | NeuA (2 entities in total) |
| Functional Keywords | carbohydrate synthesis, pseudaminic acid synthesis, cmp-transferase, transferase |
| Biological source | Aeromonas caviae |
| Total number of polymer chains | 1 |
| Total formula weight | 28011.84 |
| Authors | Keenan, T.,Fascione, M.A.,Cowan, A.R.,Hemsworth, G.R. (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 Cited by 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: 39393361DOI: 10.1016/j.str.2024.09.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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