期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 78, 期 -, 页码 613-622出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798322003114
关键词
Salmonella enterica; maltose/maltodextrin-binding protein; MalE; domain-swapped dimer; maltopentaose
资金
- Natural Science Foundation of Liaoning Province [2019-MS-065]
- Key Laboratory of Marine Bioactive Substance and Modern Analysis Technology [MBSMAT-2019-05]
- Program for Liaoning Innovative Talents in University [LJQ2015030]
- Dalian High-Level Talent Innovation Program [2019CT09]
- Central Universities in China [DC201502020203, DC201502020201]
- National Research Foundation of Korea [NRF-2017M3A9F6029736, NRF-2020M3H1A1075314, NRF-2021R1I1A1A01050838]
The crystal structure of a domain-swapped dimeric MalE from Salmonella enterica (named SeMalE) in complex with maltopentaose is reported for the first time, showing a distinct structure from typical monomeric MalE family members. These findings provide new insights into maltodextrin-binding MalE proteins.
MalE is a maltose/maltodextrin-binding protein (MBP) that plays a critical role in most bacterial maltose/maltodextrin-transport systems. Previously reported wild-type MBPs are monomers comprising an N-terminal domain (NTD) and a C-terminal domain (CTD), and maltose-like molecules are recognized between the NTD and CTD and transported to the cell system. Because MBP does not undergo artificial dimerization, it is widely used as a tag for protein expression and purification. Here, the crystal structure of a domain-swapped dimeric MalE from Salmonella enterica (named SeMalE) in complex with maltopentaose is reported for the first time, and its structure is distinct from typical monomeric MalE family members. In the domain-swapped dimer, SeMalE comprises two subdomains: the NTD and CTD. The NTD and CTD of one molecule of SeMalE interact with the CTD and NTD of the partner molecule, respectively. The domain-swapped dimeric conformation was stabilized by interactions between the NTDs, CTDs and linkers from two SeMalE molecules. Additionally, a maltopentaose molecule was found to be located at the interface between the NTD and CTD of different SeMalE molecules. These results provide new insights that will improve the understanding of maltodextrin-binding MalE proteins.
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