|
KMID : 0545120180280081339
|
|
Journal of Microbiology and Biotechnology
2018 Volume.28 No. 8 p.1339 ~ p.1345
|
|
|
Structures of Zymomonas 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase with and without a Substrate Analog at the Phosphate-Binding Loop
|
|
Seo Pil-Won
Ryu Ho-Chang
Gu Do-Heon
Park Hee-Sae
Park Suk-Youl
Kim Jeong-Sun
|
|
|
Abstract
|
|
|
|
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, which catalyzes aldol cleavage and condensation reactions, has two distinct substrate-binding sites. The substrate-binding mode at the catalytic site and Schiff-base formation have been well studied. However, structural information on the phosphate-binding loop (P-loop) is limited. Zymomonas mobilis KDPG aldolase is one of the aldolases with a wide substrate spectrum. Its structure in complex with the substrate-mimicking 3-phosphoglycerate (3PG) shows that the phosphate moiety of 3PG interacts with the P-loop and a nearby conserved serine residue. 3PG-binding to the P-loop replaces water molecules aligned from the P-loop to the catalytic site, as observed in the apostructure. The extra electron density near the P-loop and comparison with other aldolases suggest the diversity and flexibility of the serine-containing loop among KDPG aldolases. These structural data may help to understand the substrate-binding mode and the broad substrate specificity of the Zymomonas KDPG aldolase.
|
|
|
KEYWORD
|
|
|
2-Keto-3-deoxy-6-phosphogluconate aldolase (KDPG), aldolase, P-loop
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|