3PDK

crystal structure of phosphoglucosamine mutase from B. anthracis

3PDK の概要

• エントリーDOI: 10.2210/pdb3pdk/pdb
• 分子名称: Phosphoglucosamine mutase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: 4-domain architecture, mixed a/b fold, phosphohexomutase, isomerase
• 由来する生物種: Bacillus anthracis (anthrax,anthrax bacterium)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102807.60

構造登録者

Mehra-Chaudhary, R.,Mick, J.,Tanner, J.J.,Henzl, M.,Beamer, L.J. (登録日: 2010-10-22, 公開日: 2011-08-24, 最終更新日: 2023-09-06)

主引用文献

Mehra-Chaudhary, R.,Mick, J.,Beamer, L.J.
Crystal Structure of Bacillus anthracis Phosphoglucosamine Mutase, an Enzyme in the Peptidoglycan Biosynthetic Pathway.
J.Bacteriol., 193:4081-4087, 2011

PubMed Abstract: Phosphoglucosamine mutase (PNGM) is an evolutionarily conserved bacterial enzyme that participates in the cytoplasmic steps of peptidoglycan biosynthesis. As peptidoglycan is essential for bacterial survival and is absent in humans, enzymes in this pathway have been the focus of intensive inhibitor design efforts. Many aspects of the structural biology of the peptidoglycan pathway have been elucidated, with the exception of the PNGM structure. We present here the crystal structure of PNGM from the human pathogen and bioterrorism agent Bacillus anthracis. The structure reveals key residues in the large active site cleft of the enzyme which likely have roles in catalysis and specificity. A large conformational change of the C-terminal domain of PNGM is observed when comparing two independent molecules in the crystal, shedding light on both the apo- and ligand-bound conformers of the enzyme. Crystal packing analyses and dynamic light scattering studies suggest that the enzyme is a dimer in solution. Multiple sequence alignments show that residues in the dimer interface are conserved, suggesting that many PNGM enzymes adopt this oligomeric state. This work lays the foundation for the development of inhibitors for PNGM enzymes from human pathogens.

PubMed: 21685296
DOI: 10.1128/JB.00418-11

実験手法

X-RAY DIFFRACTION (2.7 Å)