Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli
| Autor: | Yongxiang Gao, Xiaoting Qiu, Ye Yuan |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Ribonucleotide
Molecular Sequence Data Biophysics Gene Expression Biology Crystallography X-Ray medicine.disease_cause Biochemistry Phosphoribosylaminoimidazolecarboxamide Formyltransferase law.invention chemistry.chemical_compound Structural Biology law Escherichia coli Genetics medicine Animals Humans Amino Acid Sequence Crystallization Bifunctional Purine metabolism Peptide sequence Space group Condensed Matter Physics Crystallography chemistry Crystallization Communications IMP cyclohydrolase activity Sequence Alignment |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:1590-1594 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309111039960 |
| Popis: | In bacteria and eukaryotes, the last two steps of de novo purine biosynthesis are catalyzed by bifunctional purine-biosynthesis protein (PurH), which is composed of two functionally independent domains linked by a flexible region. The N-terminal domain possesses IMP cyclohydrolase activity and the C-terminal domain possesses aminoimidazole-4-carboxamide ribonucleotide transformylase activity. This study reports the expression, purification, crystallization and preliminary X-ray crystallographic analysis of PurH from Escherichia coli with an N-terminal His6 tag. The crystals diffracted to a maximum resolution of 3.05 Å and belonged to the monoclinic space group P21, with unit-cell parameters a = 76.37, b = 132.15, c = 82.64 Å, β = 111.86°. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text