Please use this identifier to cite or link to this item:
|Title:||Structure of the pseudouridine synthase RsuA from Haemophilus influenzae|
|Citation:||Matte, A., Louie, G.V., Sivaraman, J., Cygler, M., Burley, S.K. (2005). Structure of the pseudouridine synthase RsuA from Haemophilus influenzae. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 61 (4) : 350-354. ScholarBank@NUS Repository. https://doi.org/10.1107/S1744309105005920|
|Abstract:||The structure of the pseudouridine synthase RsuA from Haemophilus influenza, which catalyzes the conversion of uridine to pseudouridine at a single position within 16S ribosomal RNA, has been determined at 1.59 Å resolution and compared with that of Escherichia coli RsuA. The H. influenza enzyme contains an N-terminal S4-like α3β4 domain followed by a catalytic domain, as observed in the structure of E. coli RsuA. Whereas the individual domains of E. coli and H. influenza RsuA are structurally similar, their relative spatial disposition differs greatly between the two structures. The former displays an extended open conformation with no direct contacts between the domains, while the latter is in a closed conformation with a large interface between the two domains. Domain closure presents several basic and polar residues into a putative RNA-binding cleft. It is proposed that this relative repositioning of the S4 and catalytic domains is used to modulate the shape and size of the rRNA-binding site in RsuA and in other pseudouridine synthases possessing S4 domains. © 2005 International Union of Crystallography All rights reserved.|
|Source Title:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Sep 20, 2018
WEB OF SCIENCETM
checked on Sep 4, 2018
checked on Aug 10, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.