4C21

L-Fucose Isomerase In Complex With Fucitol

4C21 の概要

• エントリーDOI: 10.2210/pdb4c21/pdb
• 関連するPDBエントリー: 4C20 4C22 4C23 4C24 4C25
• 分子名称: L-FUCOSE ISOMERASE, MANGANESE (II) ION, FUCITOL, ... (5 entities in total)
• 機能のキーワード: fucose processing, isomerase
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• 細胞内の位置: Cytoplasm (By similarity): Q97N97
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 137086.46

構造登録者

Higgins, M.A.,Suits, M.D.L.,Marsters, C.,Boraston, A.B. (登録日: 2013-08-16, 公開日: 2013-12-11, 最終更新日: 2023-12-20)

主引用文献

Higgins, M.A.,Suits, M.D.,Marsters, C.,Boraston, A.B.
Structural and Functional Analysis of Fucose-Processing Enzymes from Streptococcus Pneumoniae.
J.Mol.Biol., 426:1469-, 2014

PubMed Abstract: Fucose metabolism pathways are present in many bacterial species and typically contain the central fucose-processing enzymes fucose isomerase (FcsI), fuculose kinase (FcsK), and fuculose-1-phosphate aldolase (FcsA). Fucose initially undergoes isomerization by FcsI producing fuculose, which is then phosphorylated by FcsK. FcsA cleaves the fuculose-1-phosphate product into lactaldehyde and dihydroxyacetone phosphate, which can be incorporated into central metabolism allowing the bacterium to use fucose as an energy source. Streptococcus pneumoniae has fucose-processing operons containing homologs of FcsI, FcsK, and FcsA; however, this bacterium appears unable to utilize fucose as an energy source. To investigate this contradiction, we performed biochemical and structural studies of the S. pneumoniae fucose-processing enzymes SpFcsI, SpFcsK, and SpFcsA. These enzymes are demonstrated to act in a sequential manner to ultimately produce dihydroxyacetone phosphate and have structural features entirely consistent with their observed biochemical activities. Analogous to the regulation of the Escherichia coli fucose utilization operon, fuculose-1-phosphate appears to act as an inducing molecule for activation of the S. pneumoniae fucose operon. Despite our evidence that S. pneumoniae appears to have the appropriate regulatory and biochemical machinery for fucose metabolism, we confirmed the inability of the S. pneumoniae TIGR4 strain to grow on fucose or on the H-disaccharide, which is the probable substrate of the transporter for the pathway. On the basis of these observations, we postulate that the S. pneumoniae fucose-processing pathway has a non-metabolic role in the interaction of this bacterium with its human host.

PubMed: 24333485
DOI: 10.1016/J.JMB.2013.12.006

実験手法

X-RAY DIFFRACTION (2.55 Å)