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Pregled bibliografske jedinice broj: 579816

The A9 core sequence from NRPS adenylation domain is relevant for thioester formation


Bučević Popović, Viljemka; Šprung, Matilda; Soldo, Barbara; Pavela-Vrančić, Maja
The A9 core sequence from NRPS adenylation domain is relevant for thioester formation // ChemBioChem : a European journal of chemical biology, 13 (2012), 13; 1913-1920 doi:10.1002/cbic.201200309 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 579816 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
The A9 core sequence from NRPS adenylation domain is relevant for thioester formation

Autori
Bučević Popović, Viljemka ; Šprung, Matilda ; Soldo, Barbara ; Pavela-Vrančić, Maja

Izvornik
ChemBioChem : a European journal of chemical biology (1439-4227) 13 (2012), 13; 1913-1920

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
adenylation domain ; biosynthesis ; conserved motif ; nonribosomal peptide synthetases ; protein engineering

Sažetak
The adenylation (A) domain in nonribosomal peptide synthetases catalyses a two-step reaction in which an amino acid is activated and then transferred to the neighbouring thiolation (T) domain. In this study, we investigated the role of the conserved A9 core sequence of the A-domain of tyrocidine synthetase 1, by analysis of single amino acid mutations in the A9 region. Mutation of an absolutely conserved proline (P490G) significantly reduced the conformational stability of the protein, as evidenced by increased susceptibility to proteolytic cleavage and denaturation. All mutant A-domains were capable of amino acid activation, but the activity in the overall reaction was reduced. Surprisingly, the S491R mutant (mutation at the first residue following the A9 motif) showed elevated overall activity compared to the wild-type protein. Our results suggest that the A9 core sequence plays a role in the second reaction step, in which it could serve as a “clip” for the proper positioning of residues important for the interaction with the T-domain, and/or stabilisation of the thioester-forming conformation.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekti:
MZOS-177-0000000-2962 - Oligomerni enzimski sustavi u sintezi bioaktivnih sekundarnih metabolita (Pavela-Vrančić, Maja, MZOS ) ( POIROT)

Ustanove:
Prirodoslovno-matematički fakultet, Split

Poveznice na cjeloviti tekst rada:

doi chemistry-europe.onlinelibrary.wiley.com

Citiraj ovu publikaciju:

Bučević Popović, Viljemka; Šprung, Matilda; Soldo, Barbara; Pavela-Vrančić, Maja
The A9 core sequence from NRPS adenylation domain is relevant for thioester formation // ChemBioChem : a European journal of chemical biology, 13 (2012), 13; 1913-1920 doi:10.1002/cbic.201200309 (međunarodna recenzija, članak, znanstveni)
Bučević Popović, V., Šprung, M., Soldo, B. & Pavela-Vrančić, M. (2012) The A9 core sequence from NRPS adenylation domain is relevant for thioester formation. ChemBioChem : a European journal of chemical biology, 13 (13), 1913-1920 doi:10.1002/cbic.201200309.
@article{article, author = {Bu\v{c}evi\'{c} Popovi\'{c}, Viljemka and \v{S}prung, Matilda and Soldo, Barbara and Pavela-Vran\v{c}i\'{c}, Maja}, year = {2012}, pages = {1913-1920}, DOI = {10.1002/cbic.201200309}, keywords = {adenylation domain, biosynthesis, conserved motif, nonribosomal peptide synthetases, protein engineering}, journal = {ChemBioChem : a European journal of chemical biology}, doi = {10.1002/cbic.201200309}, volume = {13}, number = {13}, issn = {1439-4227}, title = {The A9 core sequence from NRPS adenylation domain is relevant for thioester formation}, keyword = {adenylation domain, biosynthesis, conserved motif, nonribosomal peptide synthetases, protein engineering} }
@article{article, author = {Bu\v{c}evi\'{c} Popovi\'{c}, Viljemka and \v{S}prung, Matilda and Soldo, Barbara and Pavela-Vran\v{c}i\'{c}, Maja}, year = {2012}, pages = {1913-1920}, DOI = {10.1002/cbic.201200309}, keywords = {adenylation domain, biosynthesis, conserved motif, nonribosomal peptide synthetases, protein engineering}, journal = {ChemBioChem : a European journal of chemical biology}, doi = {10.1002/cbic.201200309}, volume = {13}, number = {13}, issn = {1439-4227}, title = {The A9 core sequence from NRPS adenylation domain is relevant for thioester formation}, keyword = {adenylation domain, biosynthesis, conserved motif, nonribosomal peptide synthetases, protein engineering} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Uključenost u ostale bibliografske baze podataka::


  • AGRICOLA
  • BIOSIS Previews (Biological Abstracts)
  • MEDLINE


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