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Crystal structure of dihydrodipicolinate reductase (PaDHDPR) from Paenisporosarcina sp. TG-14: structural basis for NADPH preference as a cofactor

Cited 3 time in wos
Cited 3 time in scopus
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dc.contributor.authorLee, Chang Woo-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorPark, Hyun-
dc.contributor.authorHaJeung Park-
dc.contributor.authorHak Jun Kim-
dc.contributor.authorHyun Ho Park-
dc.contributor.authorLee, Sung Gu-
dc.contributor.authorPark, Sun-Ha-
dc.date.accessioned2018-06-12T06:55:40Z-
dc.date.available2018-06-12T06:55:40Z-
dc.date.issued2018-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/9434-
dc.description.abstractDihydrodipicolinate reductase (DHDPR) is a key enzyme in the diaminopimelate- and lysine-synthesis pathways that reduces DHDP to tetrahydrodipicolinate. Although DHDPR uses both NADPH and NADH as a cofactor, the structural basis for cofactor specificity and preference remains unclear. Here, we report that Paenisporosarcina sp. TG-14 PaDHDPR has a strong preference for NADPH over NADH, as determined by isothermal titration calorimetry and enzymatic activity assays. We determined the crystal structures of PaDHDPR alone, with its competitive inhibitor (dipicolinate), and the ternary complex of the enzyme with dipicolinate and NADPH, with results showing that only the ternary complex had a fully closed conformation and suggesting that binding of both substrate and nucleotide cofactor is required for enzymatic activity. Moreover, NADPH binding induced local conformational changes in the N-terminal long loop (residues 34?59) of PaDHDPR, as the His35 and Lys36 residues in this loop interacted with the 2′-phosphate group of NADPH, possibly accounting for the strong preference of PaDHDPR for NADPH. Mutation of these residues revealed reduced NADPH binding and enzymatic activity, confirming their importance in NADPH binding. These findings provide insight into the mechanism of action and cofactor selectivity of this important bacterial enzyme.en_US
dc.languageEnglish-
dc.subjectMultidisciplinary Sciencesen_US
dc.subject.classificationKing Sejong Stationen_US
dc.titleCrystal structure of dihydrodipicolinate reductase (PaDHDPR) from Paenisporosarcina sp. TG-14: structural basis for NADPH preference as a cofactor-
dc.title.alternative남극 빙하미생물 유래 dihydrodipicolinate reductase 효소의 삼차구조연구: 조효소로써 NADPH를 선호하는 구조적 이유 설명-
dc.typeArticleen_US
dc.identifier.bibliographicCitationLee, Chang Woo, et al. 2018. "Crystal structure of dihydrodipicolinate reductase (PaDHDPR) from Paenisporosarcina sp. TG-14: structural basis for NADPH preference as a cofactor". <em>SCIENTIFIC REPORTS</em>, 8(1): 1-12.-
dc.citation.titleSCIENTIFIC REPORTSen_US
dc.citation.volume8en_US
dc.citation.number1en_US
dc.identifier.doi10.1038/s41598-018-26291-x-
dc.citation.startPage1en_US
dc.citation.endPage12en_US
dc.description.articleClassificationSCI-
dc.description.jcrRateJCR 2016:15.625en_US
dc.subject.keywordPaenisporosarcina sp. TG-14en_US
dc.subject.keywordX-ray crystallographyen_US
dc.subject.keywordcrystal structureen_US
dc.subject.keyworddihydrodipicolinate reductaseen_US
dc.identifier.localId2018-0051-
dc.identifier.scopusid2-s2.0-85047364671-
dc.identifier.wosid000432531400043-
Appears in Collections  
2018-2018, Development of potential candidates as antibiotics based on polar genetic resources (18-18) / Lee, Jun Hyuck
2018-2018, Polar Genomics 101 Project: Genome analysis of polar organisms and establishment of application platform (18-18) / Kim, Jin-Hyoung
2017-2018, Polar Genomics 101 Project: Genome analysis of polar organisms and establishment of application platform (17-18) / Park, Hyun
2014-2017, Studies on protein structure for the spore formation mechanism of microorganisms in polar glaciers (14-17) / Lee, Jun Hyuck
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