4A34

Crystal structure of the fucose mutarotase in complex with L-fucose from Streptococcus pneumoniae

4A34 の概要

• エントリーDOI: 10.2210/pdb4a34/pdb
• 分子名称: RBSD/FUCU TRANSPORT PROTEIN FAMILY PROTEIN, beta-L-fucopyranose, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: isomerase
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 335155.98

構造登録者

Higgins, M.A.,Boraston, A.B. (登録日: 2011-09-29, 公開日: 2011-10-12, 最終更新日: 2024-05-08)

主引用文献

Higgins, M.A.,Boraston, A.B.
Structure of the Fucose Mutarotase from Streptococcus Pneumoniae in Complex with L-Fucose
Acta Crystallogr.,Sect.F, 67:1524-, 2011

PubMed Abstract: Streptococcus pneumoniae relies on a variety of carbohydrate-utilization pathways for both colonization of its human host and full virulence during the development of invasive disease. One such pathway is the fucose-utilization pathway, a component of which is fucose mutarotase (SpFcsU), an enzyme that performs the interconversion between α-L-fucose and β-L-fucose. This protein was crystallized and its three-dimensional structure was solved in complex with L-fucose. The structure shows a complex decameric quaternary structure with a high overall degree of structural identity to Escherichia coli FcsU (EcFcsU). Furthermore, the active-site architecture of SpFcsU is highly similar to that of EcFcsU. When considered in the context of the fucose-utilization pathway found in S. pneumoniae, SpFcsU appears to link the two halves of the pathway by enhancing the rate of conversion of the product of the final glycoside hydrolysis step, β-fucose, into the substrate for the fucose isomerase, α-fucose.

PubMed: 22139157
DOI: 10.1107/S1744309111046343

実験手法

X-RAY DIFFRACTION (2.5 Å)