Crystallization in Microgravity and the Atomic-Resolution Structure of Uridine Phosphorylase from Vibrio cholerae

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Crystallization in Microgravity and the Atomic-Resolution Structure of Uridine Phosphorylase from Vibrio cholerae. / Eistrikh-Heller, P. A.; Rubinsky, S. V.; Samygina, V. R.; Gabdulkhakov, A. G.; Kovalchuk, M. V.; Mironov, A. S.; Lashkov, A. A.

в: Crystallography Reports, Том 66, № 5, 01.09.2021, стр. 777-785.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Author

Eistrikh-Heller, P. A. ; Rubinsky, S. V. ; Samygina, V. R. ; Gabdulkhakov, A. G. ; Kovalchuk, M. V. ; Mironov, A. S. ; Lashkov, A. A. / Crystallization in Microgravity and the Atomic-Resolution Structure of Uridine Phosphorylase from Vibrio cholerae. в: Crystallography Reports. 2021 ; Том 66, № 5. стр. 777-785.

BibTeX

@article{495b30f12d334a51b67e8bec47e75865,

title = "Crystallization in Microgravity and the Atomic-Resolution Structure of Uridine Phosphorylase from Vibrio cholerae",

abstract = "Abstract: Uridine phosphorylases are known as key targets for the development of new anticancer and antiparasitic agents. Crystals of uridine phosphorylase from the pathogenic bacterium Vibrio cholerae were grown in microgravity by the capillary counter-diffusion method on board of the International Space Station. The three-dimensional structure of this enzyme was determined at atomic (1.04 {\AA}) resolution (RCSB PDB ID: 6Z9Z). Alternative conformations of long fragments (β-strands and adjacent loops) of the protein molecule were found for the first time in the three-dimensional structure of uridine phosphorylase in the absence of specific bound ligands. Apparently, these alternative conformations are related to the enzyme function. Conformational analysis with Markov state models demonstrated that conformational rearrangements can occur in the ligand-free state of the enzyme.",

keywords = "PRELIMINARY-X-RAY, MOLECULAR-DYNAMICS, COMPLEX, EXPRESSION, MECHANISM, PROTEIN",

author = "Eistrikh-Heller, {P. A.} and Rubinsky, {S. V.} and Samygina, {V. R.} and Gabdulkhakov, {A. G.} and Kovalchuk, {M. V.} and Mironov, {A. S.} and Lashkov, {A. A.}",

note = "Publisher Copyright: {\textcopyright} 2021, Pleiades Publishing, Inc.",

year = "2021",

month = sep,

day = "1",

doi = "10.1134/S1063774521050059",

language = "English",

volume = "66",

pages = "777--785",

journal = "Crystallography Reports",

issn = "1063-7745",

publisher = "МАИК {"}Наука/Интерпериодика{"}",

number = "5",

}

RIS

TY - JOUR

T1 - Crystallization in Microgravity and the Atomic-Resolution Structure of Uridine Phosphorylase from Vibrio cholerae

AU - Eistrikh-Heller, P. A.

AU - Rubinsky, S. V.

AU - Samygina, V. R.

AU - Gabdulkhakov, A. G.

AU - Kovalchuk, M. V.

AU - Mironov, A. S.

AU - Lashkov, A. A.

PY - 2021/9/1

Y1 - 2021/9/1

N2 - Abstract: Uridine phosphorylases are known as key targets for the development of new anticancer and antiparasitic agents. Crystals of uridine phosphorylase from the pathogenic bacterium Vibrio cholerae were grown in microgravity by the capillary counter-diffusion method on board of the International Space Station. The three-dimensional structure of this enzyme was determined at atomic (1.04 Å) resolution (RCSB PDB ID: 6Z9Z). Alternative conformations of long fragments (β-strands and adjacent loops) of the protein molecule were found for the first time in the three-dimensional structure of uridine phosphorylase in the absence of specific bound ligands. Apparently, these alternative conformations are related to the enzyme function. Conformational analysis with Markov state models demonstrated that conformational rearrangements can occur in the ligand-free state of the enzyme.

AB - Abstract: Uridine phosphorylases are known as key targets for the development of new anticancer and antiparasitic agents. Crystals of uridine phosphorylase from the pathogenic bacterium Vibrio cholerae were grown in microgravity by the capillary counter-diffusion method on board of the International Space Station. The three-dimensional structure of this enzyme was determined at atomic (1.04 Å) resolution (RCSB PDB ID: 6Z9Z). Alternative conformations of long fragments (β-strands and adjacent loops) of the protein molecule were found for the first time in the three-dimensional structure of uridine phosphorylase in the absence of specific bound ligands. Apparently, these alternative conformations are related to the enzyme function. Conformational analysis with Markov state models demonstrated that conformational rearrangements can occur in the ligand-free state of the enzyme.

KW - PRELIMINARY-X-RAY

KW - MOLECULAR-DYNAMICS

KW - COMPLEX

KW - EXPRESSION

KW - MECHANISM

KW - PROTEIN

UR - http://www.scopus.com/inward/record.url?scp=85116331703&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/0061db3c-fe57-3d24-ab82-d1d95441aa0a/

U2 - 10.1134/S1063774521050059

DO - 10.1134/S1063774521050059

M3 - Article

AN - SCOPUS:85116331703

VL - 66

SP - 777

EP - 785

JO - Crystallography Reports

JF - Crystallography Reports

SN - 1063-7745

IS - 5

ER -

ID: 88195257