Full name: Ribosomal small subunit pseudouridine synthase A
Synonym: YejD
GI: 76364197
Orf: yejD, b2183, c2720, z3442, ECs3075, SF2270, S2399
COG: COG1187
UniProt: P0AA43
Structures: | 1KSV | 1KSL | 1KSK |
Complex:
Enzyme type: pseudouridine synthase
Position of modification - modification: s:516(516) - Y

Comments:

RsuA catalyzes formation of pseudouridine at position 516 in hairpin 18 of 16S rRNA during assembly of the 30S ribosomal subunit. RsuA does not react with free unmodified 16S RNA, and only poorly with 30S particles containing unmodified RNA. The preferred substrate is an RNA fragment from residues 1 to 678 which has been complexed with 30S ribosomal proteins, suggesting that Y516 formation in vivo occurs at an intermediate stage of 30S assembly. RsuA consists of an N-terminal domain connected by an extended linker to the central and C-terminal domains. The N-terminal domain shows structural similarity to the ribosomal protein S4. RsuA is very similar in both catalytic domain structure and active site arrangement to the pseudouridine synthases RluD, TruB, and TruA, including the position of a catalytic Asp.

Protein sequence:

MRLDKFIAQQLGVSRAIAGREIRGNRVTVDGEIVRNAAFKLLPEHDVAYDGNPLAQQHGPRYFMLNKPQG YVCSTDDPDHPTVLYFLDEPVAWKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPV ADDTAEQFAKGVQLHNEKDLTKPAVLEVITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGGITL DADLAPGEYRPLTEEEIASVV

Enzymatic activities:

Reaction Substrate Type Position
U:Y rRNA (r) SSU/16S/prokaryotic cytosol 516

Publications:

Title Authors Journal Details PubMed Id DOI
Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli. Wrzesinski J, Bakin A, Nurse K, Lane BG, Ofengand J Biochemistry [details] 7612632 -
16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: deletion, mutation of the conserved Asp102 residue, and sequence comparison among all other pseudouridine synthases. Conrad J, Niu L, Rudd K, Lane BG, Ofengand J RNA [details] 10376875 -
Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP. Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A Nat Struct Biol [details] 11953756 -
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