Pretražite po imenu i prezimenu autora, mentora, urednika, prevoditelja

Napredna pretraga

Pregled bibliografske jedinice broj: 475695

Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis


Bučević-Popović, Viljemka; Šprung, Matilda; Soldo, Barbara; Orhanović, Stjepan; Pavela-Vrančić, Maja
Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis // Abstract of the 35th FEBS Congres, The FEBS Journal Volume 277 Supplement 1 / Perham, Richard et al. (ur.).
Oxford: Wiley-Blackwell, 2010. str. 190-190 (poster, međunarodna recenzija, sažetak, znanstveni)


CROSBI ID: 475695 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis

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

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Abstract of the 35th FEBS Congres, The FEBS Journal Volume 277 Supplement 1 / Perham, Richard et al. - Oxford : Wiley-Blackwell, 2010, 190-190

Skup
35th FEBS Congress: Molecules of life

Mjesto i datum
Goteborg, Švedska, 26.06.-01.07.2010

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
adenylation domain; peptide synthetase

Sažetak
Non-ribosomal peptide synthetases (NRPS) are molecular machines that synthesize peptide-based natural products, many of which are important pharmaceuticals with antibiotic, immunosuppressor and antitumor activities. A typical NRPS assembly line consists of a number of catalytic modules, each responsible for the incorporation of a single amino acid into the growing peptide product. Modules themselves comprise distinct catalytic domains, such as the adenylation domain (A) that, firstly, selects a specific amino acid monomer to be activated by ATP and, secondly, transfers it to the phosphopantetheinyl arm of the adjacent thiolation domain. Recent biochemical and structural evidence support the idea that the A domain uses a rotational movement of its two subdomains to adapt a single active site for the two partial reactions in the catalytic cycle. It has long been recognized that A domains share a set of 10 conserved motifs (A1-A10), most of which where assigned a particular role in substrate binding and/or catalysis. To our knowledge, this is the first study aimed at elucidating the role of the A9 motif. By analyzing homology models of the A domain from tyrocidine synthetase 1 from Bacillus brevis, it could be observed that during the rotational movement of the subdomains, the A9 motif drastically changes its position relative to the active site. The role of the conserved amino acid residues in this region and its importance for the two partial reactions of the catalytic cycle was examined by site-directed mutagenesis and biochemical characterization of mutant enzymes.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

Napomena
Poster odabran za kratko usmeno priopćenje



POVEZANOST RADA


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

Ustanove:
Prirodoslovno-matematički fakultet, Split


Citiraj ovu publikaciju:

Bučević-Popović, Viljemka; Šprung, Matilda; Soldo, Barbara; Orhanović, Stjepan; Pavela-Vrančić, Maja
Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis // Abstract of the 35th FEBS Congres, The FEBS Journal Volume 277 Supplement 1 / Perham, Richard et al. (ur.).
Oxford: Wiley-Blackwell, 2010. str. 190-190 (poster, međunarodna recenzija, sažetak, znanstveni)
Bučević-Popović, V., Šprung, M., Soldo, B., Orhanović, S. & Pavela-Vrančić, M. (2010) Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis. U: Perham, R. (ur.)Abstract of the 35th FEBS Congres, The FEBS Journal Volume 277 Supplement 1.
@article{article, author = {Bu\v{c}evi\'{c}-Popovi\'{c}, Viljemka and \v{S}prung, Matilda and Soldo, Barbara and Orhanovi\'{c}, Stjepan and Pavela-Vran\v{c}i\'{c}, Maja}, editor = {Perham, R.}, year = {2010}, pages = {190-190}, keywords = {adenylation domain, peptide synthetase}, title = {Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis}, keyword = {adenylation domain, peptide synthetase}, publisher = {Wiley-Blackwell}, publisherplace = {Goteborg, \v{S}vedska} }
@article{article, author = {Bu\v{c}evi\'{c}-Popovi\'{c}, Viljemka and \v{S}prung, Matilda and Soldo, Barbara and Orhanovi\'{c}, Stjepan and Pavela-Vran\v{c}i\'{c}, Maja}, editor = {Perham, R.}, year = {2010}, pages = {190-190}, keywords = {adenylation domain, peptide synthetase}, title = {Exploring the role of a conserved motif in the adenylation domain of a non-ribosomal peptide synthetase from Bacillus brevis}, keyword = {adenylation domain, peptide synthetase}, publisher = {Wiley-Blackwell}, publisherplace = {Goteborg, \v{S}vedska} }

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





Contrast
Increase Font
Decrease Font
Dyslexic Font