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C4-dicarboxylates s...
C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain
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Zhou, Yan-Feng (author)
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Nan, Beiyan (author)
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- Nan, Jie (author)
- Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory
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Ma, Qingjun (author)
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Panjikar, Santosh (author)
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Liang, Yu-He (author)
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Wang, Yiping (author)
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- Su, Xiao-Dong (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- Elsevier BV, 2008
- 2008
- English 13 s.
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In: Journal of Molecular Biology. - : Elsevier BV. - 1089-8638 .- 0022-2836. ; 383:1, s. 49-61
- Related links:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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Abstract
Subject headings
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- C(4)-dicarboxylates are the major carbon and energy sources during the symbiotic growth of rhizobia. Responses to C(4)-dicarboxylates depend on typical two-component systems (TCS) consisting of a transmembrane sensor histidine kinase and a cytoplasmic response regulator. The DctB-DctD system is the first identified TCS for C(4)-dicarboxylates sensing. Direct ligand binding to the sensor domain of DctB is believed to be the first step of the sensing events. In this report, the water-soluble periplasmic sensor domain of Sinorhizobium meliloti DctB (DctBp) was studied, and three crystal structures were solved: the apo protein, a complex with C(4) succinate, and a complex with C(3) malonate. Different from the two structurally known CitA family of carboxylate sensor proteins CitA and DcuS, the structure of DctBp consists of two tandem Per-Arnt-Sim (PAS) domains and one N-terminal helical region. Only the membrane-distal PAS domain was found to bind the ligands, whereas the proximal PAS domain was empty. Comparison of DctB, CitA, and DcuS suggests a detailed stereochemistry of C(4)-dicarboxylates ligand perception. The structures of the different ligand binding states of DctBp also revealed a series of conformational changes initiated upon ligand binding and propagated to the N-terminal domain responsible for dimerization, providing insights into understanding the detailed mechanism of the signal transduction of TCS histidine kinases.
Keyword
- Amino Acid Sequence
- Bacterial Proteins
- Crystallography, X-Ray
- Dicarboxylic Acid Transporters
- Dicarboxylic Acids
- Dimerization
- Escherichia coli Proteins
- Ligands
- Models, Molecular
- Molecular Sequence Data
- Protein Conformation
- Protein Kinases
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
- Signal Transduction
- Sinorhizobium meliloti
Publication and Content Type
- art (subject category)
- ref (subject category)
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