DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ha, Nam-Chul | ko |
dc.contributor.author | Oh, Byung-Chul | ko |
dc.contributor.author | Shin, Sejeong | ko |
dc.contributor.author | Kim, Hyun-Ju | ko |
dc.contributor.author | Oh, Tae-Kwang | ko |
dc.contributor.author | Kim, Young-Ok | ko |
dc.contributor.author | Choi, Kwan Yong | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.date.accessioned | 2013-03-03T06:34:56Z | - |
dc.date.available | 2013-03-03T06:34:56Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-02 | - |
dc.identifier.citation | NATURE STRUCTURAL BIOLOGY, v.7, no.2, pp.147 - 153 | - |
dc.identifier.issn | 1072-8368 | - |
dc.identifier.uri | http://hdl.handle.net/10203/77644 | - |
dc.description.abstract | Phytases 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.language | English | - |
dc.publisher | NATURE AMERICA INC | - |
dc.subject | BACILLUS SP. DS11 | - |
dc.subject | ASPERGILLUS-FICUUM | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | G-PROTEIN | - |
dc.subject | RESOLUTION | - |
dc.subject | CLONING | - |
dc.subject | PURIFICATION | - |
dc.subject | PHOSPHATASE | - |
dc.subject | SITE | - |
dc.title | Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states | - |
dc.type | Article | - |
dc.identifier.wosid | 000085173000017 | - |
dc.identifier.scopusid | 2-s2.0-0033950597 | - |
dc.type.rims | ART | - |
dc.citation.volume | 7 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 147 | - |
dc.citation.endingpage | 153 | - |
dc.citation.publicationname | NATURE STRUCTURAL BIOLOGY | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | Ha, Nam-Chul | - |
dc.contributor.nonIdAuthor | Oh, Byung-Chul | - |
dc.contributor.nonIdAuthor | Shin, Sejeong | - |
dc.contributor.nonIdAuthor | Kim, Hyun-Ju | - |
dc.contributor.nonIdAuthor | Oh, Tae-Kwang | - |
dc.contributor.nonIdAuthor | Kim, Young-Ok | - |
dc.contributor.nonIdAuthor | Choi, Kwan Yong | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | BACILLUS SP. DS11 | - |
dc.subject.keywordPlus | ASPERGILLUS-FICUUM | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | G-PROTEIN | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | PHOSPHATASE | - |
dc.subject.keywordPlus | SITE | - |
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