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PDBsum entry 1vio

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protein ligands Protein-protein interface(s) links
Lyase PDB id
1vio
Jmol
Contents
Protein chains
230 a.a. *
Ligands
BU1 ×4
Waters ×528
* Residue conservation analysis
PDB id:
1vio
Name: Lyase
Title: Crystal structure of pseudouridylate synthase
Structure: Ribosomal small subunit pseudouridine synthase a. Chain: a, b. Synonym: 16s pseudouridylate 516 synthase, 16s pseudouridine 516 synthase, uracil hydrolyase. Engineered: yes
Source: Haemophilus influenzae. Organism_taxid: 727. Gene: rsua, hi1243. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.59Å     R-factor:   0.196     R-free:   0.218
Authors: Structural Genomix
Key ref:
A.Matte et al. (2005). Structure of the pseudouridine synthase RsuA from Haemophilus influenzae. Acta Crystallograph Sect F Struct Biol Cryst Commun, 61, 350-354. PubMed id: 16511038 DOI: 10.1107/S1744309105005920
Date:
01-Dec-03     Release date:   30-Dec-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P45124  (RSUA_HAEIN) -  Ribosomal small subunit pseudouridine synthase A
Seq:
Struc:
232 a.a.
230 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.5.4.99.19  - 16S rRNA pseudouridine(516) synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 16S rRNA uridine516 = 16S rRNA pseudouridine516
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     RNA modification   3 terms 
  Biochemical function     isomerase activity     4 terms  

 

 
DOI no: 10.1107/S1744309105005920 Acta Crystallograph Sect F Struct Biol Cryst Commun 61:350-354 (2005)
PubMed id: 16511038  
 
 
Structure of the pseudouridine synthase RsuA from Haemophilus influenzae.
A.Matte, G.V.Louie, J.Sivaraman, M.Cygler, S.K.Burley.
 
  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 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.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 The structure of H. influenzae RsuA, showing the head-to-tail orientation of both molecules comprising the asymmetric unit. The two molecules are coloured blue and cyan or yellow and green for the catalytic and [3] [4] S4 domains, respectively. The catalytic residue (Asp102, red) is shown in atomic stick figure representation. The figure was prepared using PyMol (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System, http://www.pymol.org .]).
 
  The above figure is reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2005, 61, 350-354) copyright 2005.  
  Figure was selected by an automated process.