Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04

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dc.contributor.authorK H Park-
dc.contributor.authorJ H Jung-
dc.contributor.authorSung Goo Park-
dc.contributor.authorM E Lee-
dc.contributor.authorJ F Holden-
dc.contributor.authorC S Park-
dc.contributor.authorEui-jeon Woo-
dc.date.accessioned2017-04-19T09:54:07Z-
dc.date.available2017-04-19T09:54:07Z-
dc.date.issued2014-
dc.identifier.citationActa Crystallographica. Section D, Biological Crystallography,70,6,1659,1668ko
dc.identifier.issn09074449-
dc.identifier.uri10.1107/S1399004714006567ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12030-
dc.description.abstractA novel maltose-forming α-amylase (PSMA) was recently found in the hyperthermophilic archaeon Pyrococcus sp. ST04. This enzyme shows <13% amino-acid sequence identity to other known α-amylases and displays a unique enzymatic property in that it hydrolyzes both α-1,4-glucosidic and α-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8A is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (β/α)7-barrel fold and a C-domain (amino acids 342-597) composed of α-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is essential for specific cleavage of glucosidic bonds. The closed cavity at the active site is connected to a short substrate-binding channel that extends to the central hole of the tetramer, exhibiting a geometry that is significantly different from classical maltogenic amylases or β-amylases. The structural features of this novel exo-type maltose-forming α-amylase provide a molecular basis for its unique enzymatic characteristics and for its potential use in industrial applications and protein engineering.-
dc.publisherInt Union Crystallography-
dc.titleStructural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04-
dc.title.alternativeStructural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04-
dc.typeArticle-
dc.citation.titleActa Crystallographica Section D-Biological Crystallography-
dc.citation.number6-
dc.citation.endPage1668-
dc.citation.startPage1659-
dc.citation.volume70-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorEui-jeon Woo-
dc.contributor.alternativeName박광현-
dc.contributor.alternativeName정종현-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName이명은-
dc.contributor.alternativeNameHolden-
dc.contributor.alternativeName박천석-
dc.contributor.alternativeName우의전-
dc.identifier.bibliographicCitationActa Crystallographica Section D-Biological Crystallography, vol. 70, no. 6, pp. 1659-1668-
dc.identifier.doi10.1107/S1399004714006567-
dc.subject.keywordexo-type hydrolase-
dc.subject.keywordglycoside hydrolase family 57-
dc.subject.keywordmaltose-forming α-amylase-
dc.subject.keywordPyrococcus sp. ST04-
dc.subject.localexo-type hydrolase-
dc.subject.localglycoside hydrolase family 57-
dc.subject.localmaltose-forming α-amylase-
dc.subject.localPyrococcus sp. ST04-
dc.description.journalClassY-
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Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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