Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266, from Thermus thermophilus HB8

被引：2
|
作者：
Wong, Jaslyn E. M. M. [1 ]
Blaise, Mickael [1 ]
机构：
[1] Aarhus Univ, Dept Mol Biol & Genet, Ctr Carbohydrate Recognit & Signalling, DK-8000 Aarhus, Denmark
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金：
新加坡国家研究基金会;
关键词：
PEPTIDOGLYCAN; FEATURES; DOMAIN; PHENIX; RIPA;
D O I：
10.1107/S1744309113027164
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Autolysins belong to a protein family involved in peptidoglycan degradation and remodelling. Within this family, NlpC/P60 endopeptidases are involved in the hydrolysis of the peptide arm of peptidoglycan. In this work, the putative NlpC/P60 endopeptidase TTHA0266 from Thermus thermophilus HB8 was over-expressed, purified and crystallized. The crystals diffracted to 2.4 angstrom resolution and belonged to the hexagonal space group P6(1), with unit-cell parameters a = b = 71.19, c = 198.68 angstrom, gamma = 120 degrees. Selenomethionine-substituted protein was crystallized and the structure was solved by single-wavelength anomalous dispersion.
引用
收藏
页码：1291 / 1294
页数：4
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