PDBsum entry 1vio

Lyase

PDB id: 1vio

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

Protein chains

P45124  (RSUA_HAEIN) -  Ribosomal small subunit pseudouridine synthase A from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: 232 a.a.

Struc: 230 a.a.*

* 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.
• Reaction: uridine₅₁₆ in 16S rRNA = pseudouridine₅₁₆ in 16S rRNA

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.