دورية أكاديمية
Functional insights from the molecular modelling of a novel two-component system.
العنوان: | Functional insights from the molecular modelling of a novel two-component system. |
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المؤلفون: | Shrivastava R; Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, India., Das DR, Wiker HG, Das AK |
المصدر: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2006 Jun 16; Vol. 344 (4), pp. 1327-33. Date of Electronic Publication: 2006 May 02. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0006-291X (Print) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE |
أسماء مطبوعة: | Publication: <2002- >: San Diego, CA : Elsevier Original Publication: New York, Academic Press. |
مواضيع طبية MeSH: | Models, Molecular*, Bacterial Proteins/*chemistry , Mycobacterium tuberculosis/*enzymology , Protein Kinases/*chemistry , Trans-Activators/*chemistry, Amino Acid Sequence ; Bacterial Proteins/isolation & purification ; Computational Biology ; Histidine Kinase ; Molecular Sequence Data ; Open Reading Frames ; Phosphorylation ; Protein Conformation ; Protein Interaction Mapping ; Protein Kinases/isolation & purification ; Signal Transduction ; Trans-Activators/isolation & purification |
مستخلص: | Two-component systems (TCSs) are the major signalling pathway in bacteria and represent potential drug targets. Among the 11 paired TCS proteins present in Mycobacterium tuberculosis H37Rv, the histidine kinases (HKs) Rv0600c (HK1) and Rv0601c (HK2) are annotated to phosphorylate one response regulator (RR) Rv0602c (TcrA). We wanted to establish the sequence-structure-function relationship to elucidate the mechanism of phosphotransfer using in silico methods. Sequence alignments and codon usage analysis showed that the two domains encoded by a single gene in homologous HKs have been separated into individual open-reading frames in M. tuberculosis. This is the first example where two incomplete HKs are involved in phosphorylating a single RR. The model shows that HK2 is a unique histidine phosphotransfer (HPt)-mono-domain protein, not found as lone protein in other bacteria. The secondary structure of HKs was confirmed using "far-UV" circular dichroism study of purified proteins. We propose that HK1 phosphorylates HK2 at the conserved H131 and the phosphoryl group is then transferred to D73 of TcrA. |
المشرفين على المادة: | 0 (Bacterial Proteins) 0 (Trans-Activators) 0 (osmolarity response regulator proteins) EC 2.7.- (Protein Kinases) EC 2.7.13.1 (Histidine Kinase) |
تواريخ الأحداث: | Date Created: 20060503 Date Completed: 20060719 Latest Revision: 20161128 |
رمز التحديث: | 20240628 |
DOI: | 10.1016/j.bbrc.2006.04.019 |
PMID: | 16650822 |
قاعدة البيانات: | MEDLINE |
تدمد: | 0006-291X |
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DOI: | 10.1016/j.bbrc.2006.04.019 |