Search: onr:"swepub:oai:lup.lub.lu.se:eb25935c-2eca-44fa-afba-41ea572b2126" >
C4-dicarboxylates s...
C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain
- Article/chapterEnglish2008
Publisher, publication year, extent ...
Numbers
-
LIBRIS-ID:oai:lup.lub.lu.se:eb25935c-2eca-44fa-afba-41ea572b2126
-
https://lup.lub.lu.se/record/eb25935c-2eca-44fa-afba-41ea572b2126URI
-
https://doi.org/10.1016/j.jmb.2008.08.010DOI
Supplementary language notes
-
Language:English
-
Summary in:English
Part of subdatabase
Classification
-
Subject category:art swepub-publicationtype
-
Subject category:ref swepub-contenttype
Notes
-
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.
Subject headings and genre
-
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
Added entries (persons, corporate bodies, meetings, titles ...)
-
Nan, Beiyan
(author)
-
Nan, JieLund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory(Swepub:lu)maxl-jna
(author)
-
Ma, Qingjun
(author)
-
Panjikar, Santosh
(author)
-
Liang, Yu-He
(author)
-
Wang, Yiping
(author)
-
Su, Xiao-DongLund 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(Swepub:lu)mbfys-xs
(author)
-
Lunds universitetMAX IV-laboratoriet
(creator_code:org_t)
Related titles
-
In:Journal of Molecular Biology: Elsevier BV383:1, s. 49-611089-86380022-2836
Internet link
Find in a library
To the university's database