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

被引:4
|
作者
Smaldone, Giovanni [1 ,2 ]
Ruggiero, Alessia [1 ,3 ]
Balasco, Nicole [1 ,3 ]
Abuhammad, Areej [1 ,4 ]
Autiero, Ida [1 ,3 ]
Caruso, Daniela [1 ,5 ]
Esposito, Davide [1 ,3 ]
Ferraro, Giarita [1 ]
Gelardi, Edoardo L. M. [1 ]
Moreira, Miguel [1 ,3 ]
Quareshy, Mussa [1 ]
Romano, Maria [1 ]
Saaret, Annica [1 ]
Selvam, Irwin [1 ]
Squeglia, Flavia [1 ,3 ]
Troisi, Romualdo [1 ]
Kroon-Batenburg, Loes M. J. [1 ,6 ]
Esposito, Luciana [1 ,3 ]
Berisio, Rita [1 ,3 ]
Vitagliano, Luigi [1 ,3 ]
机构
[1] AIC Sch Crystallog Informat Fiesta 2019, Naples, Italy
[2] IRCCS SDN, Via Gianturco 113, I-80143 Naples, Italy
[3] CNR, IBB, Naples, Italy
[4] Univ Jordan, Sch Pharm, Dept Pharmaceut Sci, Amman, Jordan
[5] Univ Campania Luigi Vanvitelli, Caserta, Italy
[6] Univ Utrecht, Crystal & Struct Chem, Padualaan 8, Utrecht, Netherlands
基金
欧盟地平线“2020”;
关键词
domain swapping; protein oligomerization; protein structure dynamics; protein structure-stability; proline residue; arginine-binding protein; Thermotoga maritima; DETERMINANTS;
D O I
10.1107/S2053230X1901464X
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 (dimers, trimers and larger aggregates). The data reported here highlight the importance of evolutionary control to avoid the uncontrolled formation of heterogeneous and potentially harmful oligomeric species through domain swapping.
引用
收藏
页码:707 / 713
页数:7
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