Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D- alanine ligase (MurF) from Acinetobacter baumannii SCIE SCOPUS
DC Field | Value | Language |
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dc.contributor.author | An, Young Jun | - |
dc.contributor.author | Jeong, Chang-Sook | - |
dc.contributor.author | Yu, Jeong Hee | - |
dc.contributor.author | Chung, Kyung Min | - |
dc.contributor.author | Cha, Sun-Shin | - |
dc.date.accessioned | 2020-04-20T04:40:23Z | - |
dc.date.available | 2020-04-20T04:40:23Z | - |
dc.date.created | 2020-01-28 | - |
dc.date.issued | 2014-07 | - |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/2778 | - |
dc.description.abstract | The emergence and global spread of multidrug-resistant Acinetobacter baumannii strains are major threats to public health. Inhibition of peptidoglycan biosynthesis is an effective strategy for the development of antibiotics. The ATP-dependent UDP-N-acetylmuramoyl-tripeptide-d-alanyl-d-alanine ligase (MurF) that is responsible for the last step of peptidoglycan biosynthesis is a validated target for the development of antibiotics. Crystals of A. baumannii MurF in complex with ATP were grown by the microbatch crystallization method at 295 K. The crystals belonged to space group P3221, with unit-cell parameters a = b = 85.42, c = 129.86 angstrom. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 54.32%. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | INT UNION CRYSTALLOGRAPHY | - |
dc.title | Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D- alanine ligase (MurF) from Acinetobacter baumannii | - |
dc.type | Article | - |
dc.citation.endPage | 978 | - |
dc.citation.startPage | 976 | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.volume | 70 | - |
dc.contributor.alternativeName | 안영준 | - |
dc.contributor.alternativeName | 정창숙 | - |
dc.contributor.alternativeName | 차선신 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.976 - 978 | - |
dc.identifier.doi | 10.1107/S2053230X14009984 | - |
dc.identifier.scopusid | 2-s2.0-84905115144 | - |
dc.identifier.wosid | 000338923200027 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.subject.keywordPlus | ADDING ENZYME | - |
dc.subject.keywordPlus | PEPTIDOGLYCAN BIOSYNTHESIS | - |
dc.subject.keywordPlus | CYTOPLASMIC STEPS | - |
dc.subject.keywordPlus | EPIDEMIOLOGY | - |
dc.subject.keywordPlus | BACTEREMIA | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | PHENIX | - |
dc.subject.keywordAuthor | Acinetobacter baumannii | - |
dc.subject.keywordAuthor | MurF | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Crystallography | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |