Purification and X-ray crystallographic analysis of 7-keto-8-aminopelargonic acid (KAPA) synthase fromMycobacterium smegmatis
| Autor: | Yuan Hong, Lin Zhou, Joy Fleming, Xian-En Zhang, De-Feng Li, Tao Chen, Lijun Bi, Shanghua Fan, Da-Cheng Wang, Guanjun Chen |
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| Rok vydání: | 2014 |
| Předmět: |
Stereochemistry
Molecular Sequence Data Mycobacterium smegmatis Biophysics Crystallography X-Ray Biochemistry Chromatography Affinity law.invention chemistry.chemical_compound Bacterial Proteins Structural Biology law Genetics Amino Acid Sequence Crystallization Pyridoxal Peptide sequence chemistry.chemical_classification ATP synthase biology Condensed Matter Physics biology.organism_classification Solvent Crystallography Enzyme chemistry Crystallization Communications Acyltransferases biology.protein |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 70:1372-1375 |
| ISSN: | 2053-230X |
| Popis: | 7-Keto-8-aminopelargonic acid synthase (KAPA synthase; BioF) is an essential enzyme for mycobacterial growth that catalyses the first committed step in the biotin-synthesis pathway. It is a pyridoxal 5′-phosphate (PLP)-dependent enzyme and is a potential drug target. Here, the cloning, expression, purification and crystallization of KAPA synthase fromMycobacterium smegmatis(MsBioF) and the characterization of MsBioF crystals using X-ray diffraction are described. The crystals diffracted to 2.3 Å resolution and belonged to the monoclinic space groupP21, with unit-cell parametersa= 70.88,b= 91.68,c= 109.84 Å, β = 97.8°. According to the molecular weight of MsBioF, the unit-cell parameters and the self-rotation function map, four molecules are present in each asymmetric unit with aVMvalue of 2.06 Å3 Da−1and a solvent content of 40.20%. |
| Databáze: | OpenAIRE |
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