Crystal structure of Lon protease
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 정창숙 | - |
dc.contributor.author | 안영준 | - |
dc.contributor.author | 김민규 | - |
dc.contributor.author | 이상민 | - |
dc.contributor.author | 차선신 | - |
dc.date.accessioned | 2020-07-16T11:51:20Z | - |
dc.date.available | 2020-07-16T11:51:20Z | - |
dc.date.created | 2020-02-11 | - |
dc.date.issued | 2012-09-21 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/27564 | - |
dc.description.abstract | Lon proteases are distributed in all kingdoms of life and are required for survival of cells under stress. Lon is a tandem fusion of an AAA+ molecular chaperone and a protease with a serine-lysine catalytic dyad. We report the 2.0-Å resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating AAA+ domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts, reflecting intramolecular dynamics during ATP-driven protein unfolding and translocation. The bowl-shaped proteolytic chamber is contiguous with the chaperone chamber allowing internalized proteins direct access to the proteolytic sites without further gating restrictions.g; resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating AAA+ domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts, reflecting intramolecular dynamics during ATP-driven protein unfolding and translocation. The bowl-shaped proteolytic chamber is contiguous with the chaperone chamber allowing internalized proteins direct access to the proteolytic sites without further gating restrictions. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | European | - |
dc.relation.isPartOf | 27th European Crystallographic Meeting | - |
dc.title | Crystal structure of Lon protease | - |
dc.type | Conference | - |
dc.citation.endPage | 184 | - |
dc.citation.startPage | 184 | - |
dc.citation.title | 27th European Crystallographic Meeting | - |
dc.contributor.alternativeName | 정창숙 | - |
dc.contributor.alternativeName | 안영준 | - |
dc.contributor.alternativeName | 김민규 | - |
dc.contributor.alternativeName | 이상민 | - |
dc.contributor.alternativeName | 차선신 | - |
dc.identifier.bibliographicCitation | 27th European Crystallographic Meeting, pp.184 | - |
dc.description.journalClass | 1 | - |