6JKU

Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida

6JKU の概要

• エントリーDOI: 10.2210/pdb6jku/pdb
• 分子名称: N-acetylglucosamine-6-phosphate deacetylase, ZINC ION, PHOSPHATE ION, ... (7 entities in total)
• 機能のキーワード: deacetylase, sialic acid catabolism pathway, metal binding protein
• 由来する生物種: Pasteurella multocida
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 174914.85

構造登録者

Manjunath, L.,Bose, S.,Subramanian, R. (登録日: 2019-03-01, 公開日: 2020-03-04, 最終更新日: 2023-11-22)

主引用文献

Manjunath, L.,Coombes, D.,Davies, J.,Dhurandhar, M.,Tiwari, V.R.,Dobson, R.C.J.,Sowdhamini, R.,Ramaswamy, S.,Bose, S.
Quaternary variations in the structural assembly of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella multocida.
Proteins, 2020

PubMed Abstract: N-acetylglucosamine 6-phosphate deacetylase (NagA) catalyzes the conversion of N-acetylglucosamine-6-phosphate to glucosamine-6-phosphate in amino sugar catabolism. This conversion is an essential step in the catabolism of sialic acid in several pathogenic bacteria, including Pasteurella multocida, and thus NagA is identified as a potential drug target. Here, we report the unique structural features of NagA from P. multocida (PmNagA) resolved to 1.95 Å. PmNagA displays an altered quaternary architecture with unique interface interactions compared to its close homolog, the Escherichia coli NagA (EcNagA). We confirmed that the altered quaternary structure is not a crystallographic artifact using single particle electron cryo-microscopy. Analysis of the determined crystal structure reveals a set of hot-spot residues involved in novel interactions at the dimer-dimer interface. PmNagA binds to one Zn ion in the active site and demonstrates kinetic parameters comparable to other bacterial homologs. Kinetic studies reveal that at high substrate concentrations (~10-fold the K ), the tetrameric PmNagA displays hysteresis similar to its distant neighbor, the dimeric Staphylococcus aureus NagA (SaNagA). Our findings provide key information on structural and functional properties of NagA in P. multocida that could be utilized to design novel antibacterials.

PubMed: 32865821
DOI: 10.1002/prot.25996

実験手法

X-RAY DIFFRACTION (1.95 Å)