Crystal Structure of Aeromonas hydrophila Cytoplasmic 5 '-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase
DC Field | Value | Language |
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dc.contributor.author | Chen, Jinli | - |
dc.contributor.author | Liu, Wei | - |
dc.contributor.author | Wang, Lulu | - |
dc.contributor.author | Shang, Fei | - |
dc.contributor.author | Chen, Yuanyuan | - |
dc.contributor.author | Lan, Jing | - |
dc.contributor.author | Gao, Peng | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.contributor.author | Quan, Chunshan | - |
dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Xu, Yongbin | - |
dc.date.accessioned | 2021-09-01T11:27:40Z | - |
dc.date.available | 2021-09-01T11:27:40Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2019-07-23 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/64073 | - |
dc.description.abstract | 5'-Methylthioadenosine/S-adenosyl-L-homocysteine (MTA/SAH) nucleosidase (MTAN) is an important enzyme in a number of critical biological processes. Mammals do not express MtaN, making this enzyme an attractive antibacterial drug target. In pathogen Aeromonas hydrophila, two MtnN subfamily genes (MtaN-1 and MtaN-2) play important roles in the periplasm and cytosol, respectively. We previously reported structural and functional analyses of MtaN-1, but little is known regarding MtaN-2 due to the lack of a crystal structure. Here, we determined the crystal structure of cytosolic A. hydrophila MtaN-2 in complex with adenine (ADE), which is a cleavage product of adenosine. AhMtaN-1 and AhMtaN-2 exhibit a high degree of similarity in the alpha-beta-alpha sandwich fold of the core structural motif. However, there is a structural difference in the nonconserved extended loop between beta 7 and alpha 3 that is associated with the channel depth of the substrate-binding pocket and dimerization. The ADE molecules in the substrate-binding pockets of AhMtaN-1 and AhMtaN-2 are stabilized with pi-pi stacking by Trp199 and Phe152, respectively, and the hydrophobic residues surrounding the ribose-binding sites differ. A structural comparison of AhMtaN-2 with other MtaN proteins showed that MtnN subfamily proteins exhibit a unique substrate-binding surface and dimerization interface. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | QUORUM-SENSING SIGNAL | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | METHYLTHIOADENOSINE | - |
dc.subject | INHIBITOR | - |
dc.subject | COMPLEXES | - |
dc.subject | MECHANISM | - |
dc.subject | PHENIX | - |
dc.title | Crystal Structure of Aeromonas hydrophila Cytoplasmic 5 '-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Nam, Ki Hyun | - |
dc.identifier.doi | 10.1021/acs.biochem.9b00174 | - |
dc.identifier.scopusid | 2-s2.0-85070182931 | - |
dc.identifier.wosid | 000477093100002 | - |
dc.identifier.bibliographicCitation | BIOCHEMISTRY, v.58, no.29, pp.3136 - 3143 | - |
dc.relation.isPartOf | BIOCHEMISTRY | - |
dc.citation.title | BIOCHEMISTRY | - |
dc.citation.volume | 58 | - |
dc.citation.number | 29 | - |
dc.citation.startPage | 3136 | - |
dc.citation.endPage | 3143 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | QUORUM-SENSING SIGNAL | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | METHYLTHIOADENOSINE | - |
dc.subject.keywordPlus | INHIBITOR | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | PHENIX | - |
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