The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima

Domain swapping is a widespread oligomerization process that is observed in a large variety of protein families. In the large superfamily of substrate-binding proteins, non-monomeric members have rarely been reported. The arginine-binding protein from Thermotoga maritima (TmArgBP), a protein endowed with a number of unusual properties, presents a domain-swapped structure in its dimeric native state in which the two polypeptide chains mutually exchange their C-terminal helices. It has previously been shown that mutations in the region connecting the last two helices of the TmArgBP structure lead to the formation of a variety of oligomeric states (monomers, dimers, trimers and larger aggregates). With the aim of defining the structural determinants of domain swapping in TmArgBP, the monomeric form of the P235GK mutant has   been structurally characterized. Analysis of this arginine-bound structure indicates that it consists of a closed monomer with its C-terminal helix folded against the rest of the protein, as typically observed for substrate-binding proteins. Notably, the two terminal helices are joined by a single nonhelical residue (Gly235). Collectively, the present findings indicate that extending the hinge region and conferring it with more conformational freedom makes the formation of a closed TmArgBP monomer possible. On the other hand, the short connection between the helices may explain the tendency of the protein to also adopt alternative oligomeric states (dim...
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: domain swapping protein oligomerization protein structure dynamics – stability proline residue arginine-binding protein Thermotoga maritima research communications Source Type: research

Related Links:

Publication date: Available online 25 February 2020Source: MitochondrionAuthor(s): Viraj Muthye, Dennis V. Lavrov
Source: Mitochondrion - Category: Biochemistry Source Type: research
Publication date: Available online 24 February 2020Source: MitochondrionAuthor(s): Deepika Kundu, Ritu Pasrija
Source: Mitochondrion - Category: Biochemistry Source Type: research
Publication date: Available online 24 February 2020Source: Microvascular ResearchAuthor(s): A. Alper Öztürk, İrem Namlı, Kadri Güleç, H. Tuba Kıyan
Source: Microvascular Research - Category: Biochemistry Source Type: research
Publication date: Available online 25 February 2020Source: Polymer TestingAuthor(s): Cijun Shuai, Xun Yuan, Wenjing Yang, Shuping Peng, Chongxian He, Pei Feng, Fangwei Qi, Guoyong Wang
Source: Polymer Testing - Category: Chemistry Source Type: research
Publication date: Available online 25 February 2020Source: Polymer TestingAuthor(s): Sattaiah Naidu K, Abhijeet S. Kate, Vikas Kshirsagar, R. Ganeshan, Tukaram Gunale, Bing Zhou, Samir Anapat, Yusuf Sulub, Arun Kumar, Narayana Rao
Source: Polymer Testing - Category: Chemistry Source Type: research
Publication date: April 2020Source: Phytochemistry Letters, Volume 36Author(s): Zeynep Dogan, Kan’ichiro Ishiuchi, Toshiaki Makino, Iclal Saracoglu
Source: Phytochemistry Letters - Category: Chemistry Source Type: research
Publication date: Available online 24 February 2020Source: Computational and Theoretical ChemistryAuthor(s): F. Paularokiadoss, A. Sekar, Thayalaraj Christopher Jeyakumar
Source: Computational and Theoretical Chemistry - Category: Chemistry Source Type: research
Soft Matter, 2020, Advance Article DOI: 10.1039/C9SM02494H, PaperGhazi Ben Messaoud, Patrick Le Griel, Daniel Hermida-Merino, Niki Baccile The structure-properties relationship of lipid lamellar hydrogels composed of a biobased microbial glucolipid biosurfactant is studied against pH, temperature and shear rate usingin situ rheo-SAXS experiments. To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry
Source: RSC - Soft Matter latest articles - Category: Chemistry Authors: Source Type: research
Soft Matter, 2020, Accepted Manuscript DOI: 10.1039/D0SM00001A, Review ArticleCharles E Sing, Sarah L Perry Complex coacervation is an associative, liquid-liquid phase separation that can occur in solutions of oppositely-charged macromolecular species, such as proteins, polymers, and colloids. This process results in a coacervate phase,... The content of this RSS Feed (c) The Royal Society of Chemistry
Source: RSC - Soft Matter latest articles - Category: Chemistry Authors: Source Type: research
Phys. Chem. Chem. Phys., 2020, Accepted Manuscript DOI: 10.1039/C9CP05699H, PaperMeng-Meng Wang, Yan-Xia Zhao, Xun-Lei Ding, Wei Li, Sheng-Gui He The ability of transition metals to activate methane is quite different, and it is attractive to find the most suitable metal for the direct conversion of methane to value-added chemicals.... The content of this RSS Feed (c) The Royal Society of Chemistry
Source: RSC - Phys. Chem. Chem. Phys. latest articles - Category: Chemistry Authors: Source Type: research
More News: Biochemistry