Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states

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dc.contributor.authorHa, Nam-Chulko
dc.contributor.authorOh, Byung-Chulko
dc.contributor.authorShin, Sejeongko
dc.contributor.authorKim, Hyun-Juko
dc.contributor.authorOh, Tae-Kwangko
dc.contributor.authorKim, Young-Okko
dc.contributor.authorChoi, Kwan Yongko
dc.contributor.authorOh, Byung-Hako
dc.date.accessioned2013-03-03T06:34:56Z-
dc.date.available2013-03-03T06:34:56Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2000-02-
dc.identifier.citationNATURE STRUCTURAL BIOLOGY, v.7, no.2, pp.147 - 153-
dc.identifier.issn1072-8368-
dc.identifier.urihttp://hdl.handle.net/10203/77644-
dc.description.abstractPhytases hydrolyze phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. A thermostable phytase is of great value in applications for improving phosphate and metal ion availability in animal feed, and thereby reducing phosphate pollution to the environment. Here, we report a new folding architecture of a six-bladed propeller for phosphatase activity revealed by the 2.1 Angstrom crystal structures of a novel, thermostable phytase determined in both the partially and fully Ca2+-loaded states. Binding of two calcium ions to high-affinity calcium binding sites results in a dramatic increase in thermostability (by as much as similar to 30 degrees C in melting temperature) by joining loop segments remote in the amino acid sequence. Binding of three additional calcium ions to low-affinity calcium binding sites at the top of the molecule turns on the catalytic activity of the enzyme by converting the highly negatively charged cleft into a favorable environment for the binding of phytate.-
dc.languageEnglish-
dc.publisherNATURE AMERICA INC-
dc.subjectBACILLUS SP. DS11-
dc.subjectASPERGILLUS-FICUUM-
dc.subjectESCHERICHIA-COLI-
dc.subjectG-PROTEIN-
dc.subjectRESOLUTION-
dc.subjectCLONING-
dc.subjectPURIFICATION-
dc.subjectPHOSPHATASE-
dc.subjectSITE-
dc.titleCrystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states-
dc.typeArticle-
dc.identifier.wosid000085173000017-
dc.identifier.scopusid2-s2.0-0033950597-
dc.type.rimsART-
dc.citation.volume7-
dc.citation.issue2-
dc.citation.beginningpage147-
dc.citation.endingpage153-
dc.citation.publicationnameNATURE STRUCTURAL BIOLOGY-
dc.contributor.localauthorOh, Byung-Ha-
dc.contributor.nonIdAuthorHa, Nam-Chul-
dc.contributor.nonIdAuthorOh, Byung-Chul-
dc.contributor.nonIdAuthorShin, Sejeong-
dc.contributor.nonIdAuthorKim, Hyun-Ju-
dc.contributor.nonIdAuthorOh, Tae-Kwang-
dc.contributor.nonIdAuthorKim, Young-Ok-
dc.contributor.nonIdAuthorChoi, Kwan Yong-
dc.type.journalArticleArticle-
dc.subject.keywordPlusBACILLUS SP. DS11-
dc.subject.keywordPlusASPERGILLUS-FICUUM-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusG-PROTEIN-
dc.subject.keywordPlusRESOLUTION-
dc.subject.keywordPlusCLONING-
dc.subject.keywordPlusPURIFICATION-
dc.subject.keywordPlusPHOSPHATASE-
dc.subject.keywordPlusSITE-
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