Crystal structure of the large subunit of cobaltochelatase from Mycobacterium tuberculosis

التفاصيل البيبلوغرافية
العنوان: Crystal structure of the large subunit of cobaltochelatase from Mycobacterium tuberculosis
المؤلفون: Lin Liu, Xiao Wang, Jia‐Hui Zhang, Huai-En Dai, Min Zhang, Hui Yuan
المصدر: Proteins: Structure, Function, and Bioinformatics. 89:462-467
بيانات النشر: Wiley, 2020.
سنة النشر: 2020
مصطلحات موضوعية: Models, Molecular, Cobalamin biosynthesis, Protein subunit, Cobaltochelatase, Lyases, Crystal structure, Biochemistry, Cobalamin, Mycobacterium tuberculosis, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Protein Domains, Structural Biology, Molecular Biology, 030304 developmental biology, 0303 health sciences, Crystallography, biology, Chemistry, 030302 biochemistry & molecular biology, Significant difference, biology.organism_classification, Magnesium chelatase
الوصف: Cobaltochelatase in aerobic cobalamin biosynthesis is a complex composed of three subunits. The large subunit CobN is a 140-kDa protein and is homologous to the ChlH subunit of magnesium chelatase. Previously we have reported the 2.5-Å structure of a cyanobacterial ChlH. Here we present the 1.8-Å structure of CobN from Mycobacterium tuberculosis. The overall structure of CobN and ChlH is similar, but significant difference occurs in the head domain. Structural comparison of domains between the two proteins unravels candidate regions for substrate binding and helps to locate a triad of residues that may be essential for metal ion binding.
تدمد: 1097-0134
0887-3585
DOI: 10.1002/prot.26023
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f83cdabdf074bb515ec4f88f99523046
https://doi.org/10.1002/prot.26023
Rights: CLOSED
رقم الانضمام: edsair.doi.dedup.....f83cdabdf074bb515ec4f88f99523046
قاعدة البيانات: OpenAIRE
الوصف
تدمد:10970134
08873585
DOI:10.1002/prot.26023