Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes
DC Field | Value | Language |
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dc.contributor.author | Jang, Eun Hyuk | - |
dc.contributor.author | Lim, Jong Eun | - |
dc.contributor.author | Chi, Young Min | - |
dc.contributor.author | Lee, Ki Seog | - |
dc.date.accessioned | 2021-09-06T22:34:21Z | - |
dc.date.available | 2021-09-06T22:34:21Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2012-03 | - |
dc.identifier.issn | 2053-230X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/108993 | - |
dc.description.abstract | Succinic semialdehyde dehydrogenase (SSADH) plays a critical role in the metabolism of the inhibitory neurotransmitter ?-aminobutyric acid (GABA) and catalyzes the NAD(P)+-coupled oxidation of succinic semialdehyde (SSA) to succinic acid (SA). SSADH from Streptococcus pyogenes has been purified and crystallized as the apoenzyme and in a complex with NAD+. The crystals of native and NAD+-complexed SSADH diffracted to resolutions of 1.6 and 1.7 angstrom, respectively, using a synchrotron-radiation source. Both crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 93.3, b = 100.3, c = 105.1 angstrom for the native crystal and a = 93.3, b = 100.3, c = 105.0 angstrom for the complex crystal. Preliminary molecular replacement confirmed the presence of one dimer in both crystals, corresponding to a Matthews coefficient (VM) of 2.37 angstrom 3 Da-1 and a solvent content of 48.0%. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | INT UNION CRYSTALLOGRAPHY | - |
dc.subject | SEMI-ALDEHYDE DEHYDROGENASE | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | NMR SYSTEM | - |
dc.subject | PURIFICATION | - |
dc.subject | BRAIN | - |
dc.title | Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chi, Young Min | - |
dc.identifier.doi | 10.1107/S1744309111052055 | - |
dc.identifier.scopusid | 2-s2.0-84858959719 | - |
dc.identifier.wosid | 000301921300010 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.68, pp.288 - 291 | - |
dc.relation.isPartOf | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.volume | 68 | - |
dc.citation.startPage | 288 | - |
dc.citation.endPage | 291 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Crystallography | - |
dc.subject.keywordPlus | SEMI-ALDEHYDE DEHYDROGENASE | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | NMR SYSTEM | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | BRAIN | - |
dc.subject.keywordAuthor | succinic semialdehyde dehydrogenase | - |
dc.subject.keywordAuthor | NAD | - |
dc.subject.keywordAuthor | Streptococcus pyogenes | - |
dc.subject.keywordAuthor | GabD | - |
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