DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ryu, KS | ko |
dc.contributor.author | Kim, JI | ko |
dc.contributor.author | Cho, SJ | ko |
dc.contributor.author | Park, D | ko |
dc.contributor.author | Park, Chankyu | ko |
dc.contributor.author | Cheong, HK | ko |
dc.contributor.author | Lee, Jie-Oh | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.date.accessioned | 2009-09-24T06:12:07Z | - |
dc.date.available | 2009-09-24T06:12:07Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2005-05 | - |
dc.identifier.citation | JOURNAL OF MOLECULAR BIOLOGY, v.349, no.1, pp.153 - 162 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | http://hdl.handle.net/10203/11491 | - |
dc.description.abstract | The crystal structure of Escherichia coli rhamnose mutarotase (YiiL) is completely different from the previously reported structures of the Lactococcus lactis galactose mutarotase and the Bacillus subtilis RbsD (pyranase). YiiL exists as a locally asymmetric dimer, which is stabilized by an intermolecular b-sheet, various hydrophobic interactions, and a cation-p interaction with a salt-bridge. The protein folds of YiiL are similar to those of a Streptomyces coelicolor mono-oxygenase and a hypothetical Arabidopsis thaliana protein At3g17210. By assaying the enzymatic activity of six active-site mutants and by comparing the crystal structure-derived active site conformations of YiiL, RbsD, and a galactose mutarotase, we were able to define the amino acid residues required for catalysis and suggest a possible catalytic mechanism for YiiL. Although the active-site amino acid residues of YiiL (His, Tyr, and Trp) differ greatly from those of galactose mutarotase (His, Glu, and Asp), their geometries, which determine the structures of the preferred monosaccharide substrates, are conserved. In addition, the in vivo function of YiiL was assessed by constructing a mutant E. coli strain that carries a yiiL deletion. The presence of the yiiL gene is critical for efficient cell growth only when concentrations of L-rhamnose are limited. 2005 Elsevier Ltd. All rights reserved. | - |
dc.description.sponsorship | This work was supported, in part, by the National Creative Research Initiative Program (to B.S.C.) and by KISTEP (to C.P.). We thank undergraduate students Jaechan Kwak, Soonjoung Kim, You-ra Choi, and Yoojin Han, and graduate students Minsuk Kwon and Jeeyeon Song for generating the E. coli growth curves. We thank the staff of the Cornell High Energy Synchrotron Source (MacCHESS), the BL41XU beam line of Spring 8 and the 6B beam line of Pohang Accelerator Laboratory for help with data collection. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD | - |
dc.subject | X-RAY-DIFFRACTION | - |
dc.subject | GALACTOSE MUTAROTASE | - |
dc.subject | LACTOCOCCUS-LACTIS | - |
dc.subject | SUGAR-BINDING | - |
dc.subject | PROTEIN | - |
dc.subject | NMR | - |
dc.subject | IDENTIFICATION | - |
dc.subject | RESOLUTION | - |
dc.subject | ISOMERASE | - |
dc.subject | KINETICS | - |
dc.title | Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase | - |
dc.type | Article | - |
dc.identifier.wosid | 000229325100012 | - |
dc.identifier.scopusid | 2-s2.0-18144427117 | - |
dc.type.rims | ART | - |
dc.citation.volume | 349 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 153 | - |
dc.citation.endingpage | 162 | - |
dc.citation.publicationname | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.identifier.doi | 10.1016/j.jmb.2005.03.047 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Park, Chankyu | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.nonIdAuthor | Ryu, KS | - |
dc.contributor.nonIdAuthor | Kim, JI | - |
dc.contributor.nonIdAuthor | Cho, SJ | - |
dc.contributor.nonIdAuthor | Park, D | - |
dc.contributor.nonIdAuthor | Cheong, HK | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | monosaccharide | - |
dc.subject.keywordAuthor | mutarotase | - |
dc.subject.keywordAuthor | rhamnose | - |
dc.subject.keywordAuthor | structure | - |
dc.subject.keywordAuthor | YiiL | - |
dc.subject.keywordPlus | X-RAY-DIFFRACTION | - |
dc.subject.keywordPlus | GALACTOSE MUTAROTASE | - |
dc.subject.keywordPlus | LACTOCOCCUS-LACTIS | - |
dc.subject.keywordPlus | SUGAR-BINDING | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | NMR | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | ISOMERASE | - |
dc.subject.keywordPlus | KINETICS | - |
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