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https://doi.org/10.5562/cca3345

Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry

Justyna Czyrko ; Laboratory of Biochemistry and Structural Biology, Institute of Chemistry, University of Bialystok, Poland
Mariusz Jaskolski ; Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland
Krzysztof Brzezinski   ORCID icon orcid.org/0000-0001-9339-7745 ; Laboratory of Biochemistry and Structural Biology, Institute of Chemistry, University of Bialystok, Poland

Puni tekst: engleski, pdf (6 MB) str. 153-162 preuzimanja: 276* citiraj
APA 6th Edition
Czyrko, J., Jaskolski, M. i Brzezinski, K. (2018). Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry. Croatica Chemica Acta, 91 (2), 153-162. https://doi.org/10.5562/cca3345
MLA 8th Edition
Czyrko, Justyna, et al. "Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry." Croatica Chemica Acta, vol. 91, br. 2, 2018, str. 153-162. https://doi.org/10.5562/cca3345. Citirano 28.02.2021.
Chicago 17th Edition
Czyrko, Justyna, Mariusz Jaskolski i Krzysztof Brzezinski. "Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry." Croatica Chemica Acta 91, br. 2 (2018): 153-162. https://doi.org/10.5562/cca3345
Harvard
Czyrko, J., Jaskolski, M., i Brzezinski, K. (2018). 'Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry', Croatica Chemica Acta, 91(2), str. 153-162. https://doi.org/10.5562/cca3345
Vancouver
Czyrko J, Jaskolski M, Brzezinski K. Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry. Croatica Chemica Acta [Internet]. 2018 [pristupljeno 28.02.2021.];91(2):153-162. https://doi.org/10.5562/cca3345
IEEE
J. Czyrko, M. Jaskolski i K. Brzezinski, "Crystal Structure of S-adenosyl-L-homocysteine Hydrolase from Cytophaga hutchinsonii, a Case of Combination of Crystallographic and Non-crystallographic Symmetry", Croatica Chemica Acta, vol.91, br. 2, str. 153-162, 2018. [Online]. https://doi.org/10.5562/cca3345

Sažetak
The majority of living organisms utilize S-adenosyl-L-homocysteine hydrolase (SAHase) as a key regulator of cellular methylation reactions. The unusual evolution history of SAHase genes is reflected in the phylogeny of these proteins, which are grouped into two major domains: mainly archaeal and eukaryotic/bacterial. Such a phylogeny is in contradiction to the three-domain topology of the tree of life, commonly based on 16S rRNA sequences. Within the latter domain, SAHases are classified as eukaryotic-only or bacterial-only clades depending on their origin and sequence peculiarities. A rare exception in this classification is SAHase from a cellulose-utilizing soil bacterium Cytophaga hutchinsonii (ChSAHase), as the phylogenetic analyses indicate that ChSAHase belongs to the animal clade. Here, the P21212 crystal structure of recombinant ChSAHase in ternary complex with the oxidized form of the NAD+ cofactor and a reaction product/substrate (adenosine) is presented. Additionally, a sodium cation was identified in close proximity of the active site. The crystal contains two translational NCS-related intimate dimers of ChSAHase subunits in the asymmetric unit. Two complete tetrameric enzyme molecules are generated from these dimers within the crystal lattice through the operation of crystallographic twofold axes in the z direction.

Creative Commons License This work is licensed under a Creative Commons Attribution 4.0 International License.

Ključne riječi
cellular methylation; S-adenosyl-L-homocysteine (SAH); S-adenosyl-L-methionine (SAM); cellulose degradation; X-ray crystallography; crystallographic symmetry; non-crystallographic symmetry (NCS); translational non-crystallographic symmetry (tNCS)

Hrčak ID: 201344

URI
https://hrcak.srce.hr/201344

Posjeta: 506 *