Počet záznamů: 1
The crystal structure of XdpB, the bacterial old yellow enzyme, in an FMN-free form
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SYSNO ASEP 0489548 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The crystal structure of XdpB, the bacterial old yellow enzyme, in an FMN-free form Tvůrce(i) Zahradník, Jiří (MBU-M) ORCID
Kolenko, P. (CZ)
Palyzová, Andrea (MBU-M) RID, ORCID
Černý, J. (CZ)
Kolářová, L. (CZ)
Kyslíková, Eva (MBU-M)
Marešová, Helena (MBU-M) RID, ORCID
Grulich, Michal (MBU-M) RID
Nunvář, J. (CZ)
Šulc, M. (CZ)
Kyslík, Pavel (MBU-M) RID, ORCID
Schneider, B. (CZ)Číslo článku e0195299 Zdroj.dok. PLoS ONE. - : Public Library of Science - ISSN 1932-6203
Roč. 13, č. 4 (2018)Poč.str. 18 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova GLYCEROL TRINITRATE REDUCTASE ; N-ETHYLMALEIMIDE REDUCTASE ; OXIDATIVE STRESS-RESPONSE Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology Institucionální podpora MBU-M - RVO:61388971 UT WOS 000429505000037 EID SCOPUS 85045154045 DOI 10.1371/journal.pone.0195299 Anotace Old Yellow Enzymes (OYES) are NAD(P)H dehydrogenases of not fully resolved physiological roles that are widespread among bacteria, plants, and fungi and have a great potential for biotechnological applications. We determined the apo form crystal structure of a member of the OYE class, glycerol trinitrate reductase XdpB, from Agrobacterium bohemicum R89-1 at 2.1 A resolution. In agreement with the structures of the related bacterial OYEs, the structure revealed the TIM barrel fold with an N-terminal beta-hairpin lid, but surprisingly, the structure did not contain its cofactor FMN. Its putative binding site was occupied by a pentapeptide TTSDN from the C-terminus of a symmetry related molecule. Biochemical experiments confirmed a specific concentration-dependent oligomerization and a low FMN content. The blocking of the FMN binding site can exist in vivo and regulates enzyme activity. Our bioinformatic analysis indicated that a similar self-inhibition could be expected in more OYEs which we designated as subgroup OYE C1. This subgroup is widespread among G-bacteria and can be recognized by the conserved sequence GxxDYP in proximity of the C termini. In proteobacteria, the C1 subgroup OYEs are typically coded in one operon with short-chain dehydrogenase. This operon is controlled by the tetR-like transcriptional regulator. OYEs coded in these operons are unlikely to be involved in the oxidative stress response as the other known members of the OYE family because no upregulation of XdpB was observed after exposing A. bohemicum R89-1 to oxidative stress. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2019
Počet záznamů: 1