Počet záznamů: 1
Adaptation of an L-Proline Adenylation Domain to Use 4-Propyl-L-Proline in the Evolution of Lincosamide Biosynthesis
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SYSNO ASEP 0425633 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Adaptation of an L-Proline Adenylation Domain to Use 4-Propyl-L-Proline in the Evolution of Lincosamide Biosynthesis Tvůrce(i) Kadlčík, Stanislav (MBU-M) RID, ORCID
Kučera, Tomáš (MBU-M)
Chalupská, Dominika (MBU-M)
Gažák, Radek (MBU-M) RID, ORCID
Koběrská, Markéta (MBU-M) ORCID
Ulanová, Dana (MBU-M)
Kopecký, Jan (MBU-M)
Kutejová, Eva (MBU-M) RID
Najmanová, Lucie (MBU-M) RID
Janata, Jiří (MBU-M) RID, ORCIDZdroj.dok. PLoS ONE. - : Public Library of Science - ISSN 1932-6203
Roč. 8, č. 12 (2013)Poč.str. 16 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova NONRIBOSOMAL PEPTIDE SYNTHETASES ; GENE-CLUSTER ; BIOCHEMICAL-CHARACTERIZATION Vědní obor RIV EE - Mikrobiologie, virologie CEP EE2.3.20.0055 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy EE2.3.30.0003 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy ED1.1.00/02.0109 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora MBU-M - RVO:61388971 UT WOS 000329117900118 DOI 10.1371/journal.pone.0084902 Anotace Clinically used lincosamide antibiotic lincomycin incorporates in its structure 4-propyl-L-proline (PPL), an unusual amino acid, while celesticetin, a less efficient related compound, makes use of proteinogenic L-proline. Biochemical characterization, as well as phylogenetic analysis and homology modelling combined with the molecular dynamics simulation were employed for complex comparative analysis of the orthologous protein pair LmbC and CcbC from the biosynthesis of lincomycin and celesticetin, respectively. The analysis proved the compared proteins to be the standalone adenylation domains strictly preferring their own natural substrate, PPL or L-proline. The LmbC substrate binding pocket is adapted to accomodate a rare PPL precursor. When compared with L-proline specific ones, several large amino acid residues were replaced by smaller ones opening a channel which allowed the alkyl side chain of PPL to be accommodated. One of the most important differences, that of the residue corresponding to V306 in CcbC changing to G308 in LmbC, was investigated in vitro and in silico. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2014
Počet záznamů: 1