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

doi:10.1107/S2053230X1901464X

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Article

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

Acta crystallographica. Section F, Structural biology communications - 1 Nov 2019

Smaldone Giovanni, Ruggiero Alessia, Balasco Nicole, Abuhammad Areej, Autiero Ida, Caruso Daniela, Esposito Davide, Ferraro Giarita, Gelardi Edoardo L M, Moreira Miguel, Quareshy Mussa, Romano Maria, Saaret Annica, Selvam Irwin, Squeglia Flavia, Troisi Romualdo, Kroon-Batenburg Loes M J, Esposito Luciana, Berisio Rita, Vitagliano Luigi

Abstract excerpt

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...

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Identifiers

PMID: 31702584
DOI: 10.1107/S2053230X1901464X
PMCID: PMC6839819

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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