DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hyung Jin Cha | - |
dc.contributor.author | Doo Soo Jang | - |
dc.contributor.author | Yeon -gil Kim | - |
dc.contributor.author | Bee- Hak Hong | - |
dc.contributor.author | Jae-sung Woo | - |
dc.contributor.author | Kim, KT | - |
dc.contributor.author | Choi, KY | - |
dc.date.accessioned | 2016-03-31T08:18:27Z | - |
dc.date.available | 2016-03-31T08:18:27Z | - |
dc.date.created | 2013-11-12 | - |
dc.date.issued | 2013-07 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.other | 2013-OAK-0000028841 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/15014 | - |
dc.description.abstract | Proteins have evolved to compensate for detrimental mutations. However, compensatory mechanisms for protein defects are not well understood. Using ketosteroid isomerase (KSI), we investigated how second-site mutations could recover defective mutant function and stability. Previous results revealed that the Y30F mutation rescued the Y14F, Y55F and Y14F/Y55F mutants by increasing the catalytic activity by 23-, 3- and 1.3-fold, respectively, and the Y55F mutant by increasing the stability by 3.3 kcal/mol. To better understand these observations, we systematically investigated detailed structural and thermodynamic effects of the Y30F mutation on these mutants. Crystal structures of the Y14F/Y30F and Y14F/Y55F mutants were solved at 2.0 and 1.8 previoulsy solved structures of wild-type and other mutant KSIs. Structural analyses revealed that the Y30F mutation partially restored the active-site cleft of these mutant KSIs. The Y30F mutation also increased Y14F and Y14F/Y55F mutant stability by 3.2 and 4.3 kcal/mol, respectively, and the melting temperatures of the Y14F, Y55F and Y14F/Y55F mutants by 6.4A degrees C, 5.1A degrees C and 10.0A degrees C, respectively. Compensatory effects of the Y30F mutation on stability might be due to improved hydrophobic interactions because removal of a hydroxyl group from Tyr30 induced local compaction by neighboring residue movement and enhanced interactions with surrounding hydrophobic residues in the active site. Taken together, our results suggest that perturbed active-site geometry recovery and favorable hydrophobic interactions mediate the role of Y30F as a secondsite suppressor. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | KSBMB | - |
dc.relation.isPartOf | Molecules and cells | - |
dc.subject | active-site recovery | - |
dc.subject | ketosteroid isomerase | - |
dc.subject | more hydrophobic interactions | - |
dc.subject | rescue mechanism | - |
dc.subject | second-site suppressor | - |
dc.subject | HYDROGEN-BOND NETWORK | - |
dc.subject | PUTIDA BIOTYPE-B | - |
dc.subject | ONCOGENIC P53 MUTATIONS | - |
dc.subject | DELTA(5)-3-KETOSTEROID ISOMERASE | - |
dc.subject | ACTIVE-SITE | - |
dc.subject | SUPPRESSOR MUTATIONS | - |
dc.subject | T4 LYSOZYME | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | STRUCTURAL BASIS | - |
dc.subject | DOUBLE-MUTANT | - |
dc.title | Rescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomerase | - |
dc.type | Article | - |
dc.contributor.college | 융합생명공학부 | - |
dc.identifier.doi | 10.1007/S10059-013-0013-1 | - |
dc.author.google | Cha, HJ | - |
dc.author.google | Jang, DS | - |
dc.author.google | Kim, YG | - |
dc.author.google | Hong, BH | - |
dc.author.google | Woo, JS | - |
dc.author.google | Kim, KT | - |
dc.author.google | Choi, KY | - |
dc.relation.volume | 36 | - |
dc.relation.issue | 1 | - |
dc.relation.startpage | 39 | - |
dc.relation.lastpage | 46 | - |
dc.contributor.id | 10104775 | - |
dc.relation.journal | MOLECULES AND CELLS | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCIE | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Molecules and cells, v.36, no.1, pp.39 - 46 | - |
dc.identifier.wosid | 000322118500005 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 46 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 39 | - |
dc.citation.title | Molecules and cells | - |
dc.citation.volume | 36 | - |
dc.contributor.affiliatedAuthor | Kim, KT | - |
dc.contributor.affiliatedAuthor | Choi, KY | - |
dc.identifier.scopusid | 2-s2.0-84893698071 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 7 | - |
dc.description.scptc | 7 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | HYDROGEN-BOND NETWORK | - |
dc.subject.keywordPlus | PUTIDA BIOTYPE-B | - |
dc.subject.keywordPlus | ONCOGENIC P53 MUTATIONS | - |
dc.subject.keywordPlus | DELTA(5)-3-KETOSTEROID ISOMERASE | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | SUPPRESSOR MUTATIONS | - |
dc.subject.keywordPlus | T4 LYSOZYME | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
dc.subject.keywordPlus | DOUBLE-MUTANT | - |
dc.subject.keywordAuthor | active-site recovery | - |
dc.subject.keywordAuthor | ketosteroid isomerase | - |
dc.subject.keywordAuthor | more hydrophobic interactions | - |
dc.subject.keywordAuthor | rescue mechanism | - |
dc.subject.keywordAuthor | second-site suppressor | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
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