Crystallization and Preliminary X-ray Diffraction Study of Phosphopantetheine Adenylyltransferase from M-Tuberculosis Crystallizing in Space Group P32

被引：2

作者：

Timofeev, V. I. ^{[1
,3
]}

Chupova, L. A. ^{[2
]}

Esipov, R. S. ^{[2
]}

Kuranova, I. P. ^{[1
,3
]}

机构：

[1] Russian Acad Sci, AV Shubnikov Crystallog Inst, Moscow 119333, Russia

[2] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

[3] Kurchatov Inst, Natl Res Ctr, Moscow 123098, Russia

来源：

CRYSTALLOGRAPHY REPORTS | 2015年 / 60卷 / 05期

基金：

俄罗斯基础研究基金会;

关键词：

COENZYME-A; 3-DIMENSIONAL STRUCTURE; MECHANISM; COMPLEX;

D O I：

10.1134/S106377451505017X

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

Crystals of M. tuberculosis phosphopantetheine adenylyltransferase were grown in microgravity by the capillary counter-diffusion method through a gel layer. The X-ray diffraction data set suitable for the determination of the three-dimensional structure at atomic resolution was collected from one crystal at the Spring-8 synchrotron facility to 2.00-angstrom resolution. The crystals belong to sp. gr. P3(2) and have the following unit-cell parameters: a = b = 106.47 angstrom, c = 71.32 angstrom , alpha = gamma = 90 degrees, beta = 120 degrees. The structure was solved by the molecular-replacement method. There are six subunits of the enzyme comprising a hexamer per asymmetric unit. The hexamer is a biologically active form of phosphopantetheine adenylyltransferase from M. tuberculosis.

引用

页码：682 / 684

页数：3

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