Structure of the fucose mutarotase from Streptococcus pneumoniae in complex with l-fucose

被引:6
作者
Higgins, Melanie A. [1 ]
Boraston, Alisdair B. [1 ]
机构
[1] Univ Victoria, Dept Biochem & Microbiol, Victoria, BC V8W 3P6, Canada
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷
基金
加拿大自然科学与工程研究理事会;
关键词
Streptococcus pneumoniae; mutarotases; fucose metabolism; CRYSTAL-STRUCTURES; STRUCTURE VALIDATION; ESCHERICHIA-COLI; VIRULENCE; CLONING; IDENTIFICATION; PURIFICATION; METABOLISM;
D O I
10.1107/S1744309111046343
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 a-l-fucose and beta-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, beta-fucose, into the substrate for the fucose isomerase, a-fucose.
引用
收藏
页码:1524 / 1530
页数:7
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