1vio: Difference between revisions

Revision as of 12:34, 3 May 2008

Crystal structure of pseudouridylate synthase

OverviewOverview

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 A resolution and compared with that of Escherichia coli RsuA. The H. influenza enzyme contains an N-terminal S4-like alpha3beta4 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.

About this StructureAbout this Structure

1VIO is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the pseudouridine synthase RsuA from Haemophilus influenzae., Matte A, Louie GV, Sivaraman J, Cygler M, Burley SK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):350-4. Epub 2005 Mar 12. PMID:16511038 Page seeded by OCA on Sat May 3 12:34:33 2008

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OCA

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-}}
 '''Crystal structure of pseudouridylate synthase'''
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 [[Category: Single protein]]
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+[[Category: Structural genomic]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:34:33 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:59 2008''