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恶性疟原虫核糖-5-磷酸异构酶的结构

Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.

作者信息

Holmes Margaret A, Buckner Frederick S, Van Voorhis Wesley C, Verlinde Christophe L M J, Mehlin Christopher, Boni Erica, DeTitta George, Luft Joseph, Lauricella Angela, Anderson Lori, Kalyuzhniy Oleksandr, Zucker Frank, Schoenfeld Lori W, Earnest Thomas N, Hol Wim G J, Merritt Ethan A

机构信息

Structural Genomics of Pathogenic Protozoa (SGPP) Consortium, USA.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt 5):427-31. doi: 10.1107/S1744309106010876. Epub 2006 Apr 12.

DOI:10.1107/S1744309106010876
PMID:16682767
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2219984/
Abstract

The structure of ribose 5-phosphate isomerase from Plasmodium falciparum, PFE0730c, has been determined by molecular replacement at 2.09 angstroms resolution. The enzyme, which catalyzes the isomerization reaction that interconverts ribose 5-phosphate and ribulose 5-phosphate, is a member of the pentose phosphate pathway. The P. falciparum enzyme belongs to the ribose 5-phosphate isomerase A family, Pfam family PF06562 (DUF1124), and is structurally similar to other members of the family.

摘要

恶性疟原虫的核糖-5-磷酸异构酶(PFE0730c)的结构已通过分子置换法在2.09埃分辨率下确定。该酶催化核糖-5-磷酸和核酮糖-5-磷酸相互转化的异构化反应,是磷酸戊糖途径的一员。恶性疟原虫的这种酶属于核糖-5-磷酸异构酶A家族,即Pfam家族PF06562(DUF1124),并且在结构上与该家族的其他成员相似。

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