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Crystal Structure and Functional Characterization of a Xylose Isomerase (PbXI) from the Psychrophilic Soil Microorganism, Paenibacillus sp.

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Cited 1 time in scopus
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dc.contributor.authorPark, Sun-Ha-
dc.contributor.authorKwon, Sunghark-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorKim, Chang Min-
dc.contributor.authorJeong, Chang Sook-
dc.contributor.authorKim, Kyung-Jin-
dc.contributor.authorHong, Jong Wook-
dc.contributor.authorKim, Hak Jun-
dc.contributor.authorPark, Hyun Ho-
dc.contributor.authorLee, Jun Hyuck-
dc.date.accessioned2020-10-20T02:23:48Z-
dc.date.available2020-10-20T02:23:48Z-
dc.date.issued2019-02-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/10876-
dc.description.abstractXylose isomerase (XI; E.C.5.3.1.5) catalyzes the isomerization of xylose to xylulose, which can be used to produce bioethanol through fermentation. Therefore, XI has recently gained attention as a key catalyst in the bioenergy industry. Here, we identified, purified, and characterized a XI (PbXI) from the psychrophilic soil microorganism, Paenibacillus sp. R4. Surprisingly, activity assay results showed that PbXI is not a cold-active enzyme, but displays optimal activity at 60 degrees C. We solved the crystal structure of PbXI at 1.94-angstrom resolution to investigate the origin of its thermostability. The PbXI structure shows a (beta/alpha)(8)-barrel fold with tight tetrameric interactions and it has three divalent metal ions (CaI, CaII, and CaIII). Two metal ions (CaI and CaII) located in the active site are known to be involved in the enzymatic reaction. The third metal ion (CaIII), located near the beta 4-alpha 6 loop region, was newly identified and is thought to be important for the stability of PbXI. Compared with previously determined thermostable and mesophilic XI structures, the beta 1-alpha 2 loop structures near the substrate binding pocket of PbXI were remarkably different. Site-directed mutagenesis studies suggested that the flexible beta 1-alpha 2 loop region is essential for PbXI activity. Our findings provide valuable insights that can be applied in protein engineering to generate low-temperature purpose-specific XI enzymes.en_US
dc.languageEnglishen_US
dc.language.isoenen_US
dc.subjectBiotechnology & Applied Microbiologyen_US
dc.subjectMicrobiologyen_US
dc.subject.classificationDasan Stationen_US
dc.titleCrystal Structure and Functional Characterization of a Xylose Isomerase (PbXI) from the Psychrophilic Soil Microorganism, Paenibacillus sp.en_US
dc.title.alternative알래스카 토양 미생물 유래 xylose isomerase 효소의 구조와 기능 연구en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationPark, Sun-Ha, et al. 2019. "Crystal Structure and Functional Characterization of a Xylose Isomerase (PbXI) from the Psychrophilic Soil Microorganism, Paenibacillus sp.". <em>JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY</em>, 29(2): 244-255.en_US
dc.citation.titleJOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGYen_US
dc.citation.volume29en_US
dc.citation.number2en_US
dc.identifier.doi10.4014/jmb.1810.10057-
dc.citation.startPage244en_US
dc.citation.endPage255en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2017:68.323en_US
dc.subject.keywordPaenibacillus speciesen_US
dc.subject.keywordX-ray crystallographyen_US
dc.subject.keywordcold-active proteinen_US
dc.subject.keywordcrystal structureen_US
dc.subject.keywordxylose isomeraseen_US
dc.identifier.localId2019-0007-
dc.identifier.scopusid2-s2.0-85062856066-
dc.identifier.wosid000459779100008-
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