Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium

被引：3
|
作者：
Azim, N. [1 ]
Deery, E. [2 ]
Warren, M. J. [2 ]
Erskine, P. [3 ]
Cooper, J. B. [3 ]
Wood, S. P. [3 ]
Akhtar, M. [1 ]
机构：
[1] Univ Punjab, Sch Biol Sci, Lahore 54590, Pakistan
[2] Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
[3] UCL Div Med, Lab Prot Crystallog, Ctr Amyloidosis & Acute Phase Prot, London NW3 2PF, England
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金：
英国生物技术与生命科学研究理事会;
关键词：
HYDROXYMETHYLBILANE SYNTHASE; LAUE DIFFRACTION; CATALYTIC SITE; DATA QUALITY; RESOLUTION; CRYSTALS;
D O I：
10.1107/S1744309113018526
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses an early step of the tetrapyrrole-biosynthesis pathway in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. The enzyme possesses a dipyrromethane cofactor which is covalently linked by a thioether bridge to an invariant cysteine residue. Expression in Escherichia coli of a His-tagged form of Bacillus megaterium PBGD permitted the crystallization and preliminary X-ray analysis of the enzyme from this species at high resolution.
引用
收藏
页码：906 / 908
页数：3
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