1KSV

STRUCTURE OF RSUA

Summary for 1KSV

• Entry DOI: 10.2210/pdb1ksv/pdb
• Related: 1KSK 1KSL
• Descriptor: RIBOSOMAL SMALL SUBUNIT PSEUDOURIDINE SYNTHASE A, URIDINE-5'-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: pseudouridine synthase, rsua, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 26695.35

Authors

Sivaraman, J.,Sauve, V.,Larocque, R.,Stura, E.A.,Schrag, J.D.,Cygler, M.,Matte, A. (deposition date: 2002-01-14, release date: 2002-04-24, Last modification date: 2024-10-16)

Primary citation

Sivaraman, J.,Sauve, V.,Larocque, R.,Stura, E.A.,Schrag, J.D.,Cygler, M.,Matte, A.
Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP.
Nat.Struct.Biol., 9:353-358, 2002

PubMed Abstract: In Escherichia coli, the pseudouridine synthase RsuA catalyzes formation of pseudouridine (psi) at position 516 in 16S rRNA during assembly of the 30S ribosomal subunit. We have determined the crystal structure of RsuA bound to uracil at 2.0 A resolution and to uridine 5'-monophosphate (UMP) at 2.65 A resolution. RsuA consists of an N-terminal domain connected by an extended linker to the central and C-terminal domains. Uracil and UMP bind in a cleft between the central and C-terminal domains near the catalytic residue Asp 102. The N-terminal domain shows structural similarity to the ribosomal protein S4. Despite only 15% amino acid identity, the other two domains are structurally similar to those of the tRNA-specific psi-synthase TruA, including the position of the catalytic Asp. Our results suggest that all four families of pseudouridine synthases share the same fold of their catalytic domain(s) and uracil-binding site.

PubMed: 11953756

Experimental method

X-RAY DIFFRACTION (2.65 Å)