5.4.99.23: 23S rRNA pseudouridine1911/1915/1917 synthase

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For detailed information about 23S rRNA pseudouridine1911/1915/1917 synthase, go to the full flat file.

Reaction

Synonyms

pseudouridine synthase RluD, pseudouridine synthases RluD, ribosomal large subunit pseudouridine synthase D, RluD, RluD pseudouridine synthase, sfhB, YfiI, YfiL

ECTree

     5 Isomerases

         5.4 Intramolecular transferases

             5.4.99 Transferring other groups

                5.4.99.23 23S rRNA pseudouridine1911/1915/1917 synthase

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Results	in table
902	AA Sequence
7	Cloned(Commentary)
4	Crystallization (Commentary)
11	General Information
1	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
14	Organism
1	PDB ID
4	Protein Variants
6	Purification (Commentary)
1	Reaction
14	Reference
15	Substrates and Products (Substrate)
3	Subunits
21	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Crystallization

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Crystallization on EC 5.4.99.23 - 23S rRNA pseudouridine1911/1915/1917 synthase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

2.0 A structure of the catalytic domain of RluD (residues 77–326). The catalytic domain folds into a mainly antiparallel beta-sheet flanked by several loops and helices. A positively charged cleft that presumably binds RNA leads to the conserved Asp139. The RluD N-terminal S4 domain, connected by a flexible linker, is disordered in our structure. RluD is very similar in both catalytic domain structure and active site arrangement to the pseudouridine synthases RsuA, TruB, and TruA

Escherichia coli

P33643

706712

crystallization of selenomethionine-substituted RluD by the hanging-drop method, crystals diffract to 1.9 A and belong to space group P4(3)2(1)2, with unit cell parameters a = b = 75.14, c = 181.81 A

Escherichia coli

-

649216

crystals of full-length RluD are grown at 20°C using the hanging drop method. The S4 domain of RluD appears to be highly flexible or unfolded and is completely invisible in the electron density map

Escherichia coli

P33643

702207

crystals of SeMet-labeled DELTARluD are obtained under oil by the microbatch method, crystal structure of the catalytic module of RluD (residues 68–326, DELTARluD) refined at 1.8 A to a final R-factor of 21.8%. DELTARluD is a monomeric enzyme having an overall mixed alpha/beta fold. The DELTARluD molecule consists of two subdomains, a catalytic subdomain and C-terminal subdomain with the RNA-binding cleft formed by loops extending from the catalytic sub-domain. Comparison of the structure with other pseudouridine synthases

Escherichia coli

Q8X9F0

652934