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.
In: Crystallography Reports, Vol. 66, No. 5, 01.09.2021, p. 777-785.Research output: Contribution to journal › Article › peer-review
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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.
N1 - Publisher Copyright: © 2021, Pleiades Publishing, Inc.
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