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.

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收藏

页码：906 / 908

页数：3

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