Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway
DC Field | Value | Language |
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dc.contributor.author | Kim, Min Kyung | - |
dc.contributor.author | Oh, Sun Joo | - |
dc.contributor.author | Lee, Byung-Gil | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2021-09-03T17:08:37Z | - |
dc.date.available | 2021-09-03T17:08:37Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2016-11-01 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/86880 | - |
dc.description.abstract | The first step of the hierarchically organized Arg/N-end rule pathway of protein degradation is deamidation of the N-terminal glutamine and asparagine residues of substrate proteins to glutamate and aspartate, respectively. These reactions are catalyzed by the N-terminal amidase (Nt-amidase) Nta1 in fungi such as Saccharomyces cerevisiae, and by the glutamine-specific Ntaq1 and asparagine-specific Ntan1 Nt-amidases in mammals. To investigate the dual specificity of yeast Nta1 (yNta1)and the importance of second-position residues in Asn/Gln-bearing N-terminal degradation signals (N-degrons), we determined crystal structures of yNta1 in the apo state and in complex with various N-degron peptides. Both an Asn-peptide and a Gln-peptide fit well into the hollow active site pocket of yNta1, with the catalytic triad located deeper inside the active site. Specific hydrogen bonds stabilize interactions between N-degron peptides and hydrophobic peripheral regions of the active site pocket. Key determinants for substrate recognition were identified and thereafter confirmed by using structure-based mutagenesis. We also measured affinities between yNta1 (wild-type and its mutants) and specific peptides, and determined K-M and k(cat) for peptides of each type. Together, these results elucidate, in structural and mechanistic detail, specific deamidation mechanisms in the first step of the N-end rule pathway. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | ADAPTER PROTEIN | - |
dc.subject | SUBSTRATE RECOGNITION | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | COMPONENT | - |
dc.subject | ACETYLATION | - |
dc.subject | ENZYME | - |
dc.subject | GENE | - |
dc.title | Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1073/pnas.1612620113 | - |
dc.identifier.scopusid | 2-s2.0-84994242315 | - |
dc.identifier.wosid | 000386608200046 | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.113, no.44, pp.12438 - 12443 | - |
dc.relation.isPartOf | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 113 | - |
dc.citation.number | 44 | - |
dc.citation.startPage | 12438 | - |
dc.citation.endPage | 12443 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | ADAPTER PROTEIN | - |
dc.subject.keywordPlus | SUBSTRATE RECOGNITION | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | COMPONENT | - |
dc.subject.keywordPlus | ACETYLATION | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordAuthor | dual specificity | - |
dc.subject.keywordAuthor | nitrilase superfamily | - |
dc.subject.keywordAuthor | N-end rule | - |
dc.subject.keywordAuthor | Nta1 | - |
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