Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis

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dc.contributor.authorT P Cao-
dc.contributor.authorJoong Su Kim-
dc.contributor.authorMi Hee Woo-
dc.contributor.authorJ M Choi-
dc.contributor.authorY Jun-
dc.contributor.authorK H Lee-
dc.contributor.authorS H Lee-
dc.date.accessioned2017-04-19T10:19:48Z-
dc.date.available2017-04-19T10:19:48Z-
dc.date.issued2016-
dc.identifier.issn12258873-
dc.identifier.uri10.1007/s12275-016-6029-4ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13215-
dc.description.abstract2-deoxyribose-5-phosphate aldolase (DERA) is a class I aldolase that catalyzes aldol condensation of two aldehydes in the active site, which is particularly germane in drug manufacture. Structural and biochemical studies have shown that the active site of DERA is typically loosely packed and displays broader substrate specificity despite sharing conserved folding architecture with other aldolases. The most distinctive structural feature of DERA compared to other aldolases is short and flexible C-terminal region. This region is also responsible for substrate recognition. Therefore, substrate tolerance may be related to the C-terminal structural features of DERA. Here, we determined the crystal structures of full length and C-terminal truncated DERA from Streptococcus suis (SsDERA). In common, both contained the typical (α/β)8 TIM-barrel fold of class I aldolases. Surprisingly, C-terminal truncation resulting in missing the last α9 and β8 secondary elements, allowed DERA to maintain activity comparable to the fulllength enzyme. Specifically, Arg186 and Ser205 residues at the C-terminus appeared mutually supplemental or less indispensible for substrate phosphate moiety recognition. Our results suggest that DERA might adopt a shorter C-terminal region than conventional aldolases during evolution pathway, resulting in a broader range of substrate tolerance through active site flexibility.-
dc.publisherMicrobiological Society Korea-
dc.titleStructural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis-
dc.title.alternativeStructural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis-
dc.typeArticle-
dc.citation.titleJournal of Microbiology-
dc.citation.number4-
dc.citation.endPage321-
dc.citation.startPage311-
dc.citation.volume54-
dc.contributor.affiliatedAuthorJoong Su Kim-
dc.contributor.alternativeNameCao-
dc.contributor.alternativeName김중수-
dc.contributor.alternativeName우미희-
dc.contributor.alternativeName최진명-
dc.contributor.alternativeName전영수-
dc.contributor.alternativeName이건호-
dc.contributor.alternativeName이성행-
dc.identifier.bibliographicCitationJournal of Microbiology, vol. 54, no. 4, pp. 311-321-
dc.identifier.doi10.1007/s12275-016-6029-4-
dc.subject.keyword2-deoxyribose-5-phosphate aldolase-
dc.subject.keywordClass I aldolase-
dc.subject.keywordDERA-
dc.subject.keywordS. suis-
dc.subject.keywordTIM-barrel-
dc.subject.local2-deoxyribose-5-phosphate aldolase-
dc.subject.localClass I aldolase-
dc.subject.localDERA-
dc.subject.localS. suis-
dc.subject.localTIM-barrel-
dc.description.journalClassY-
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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