Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.1.26.11: tRNase Z

This is an abbreviated version!
For detailed information about tRNase Z, go to the full flat file.

Word Map on EC 3.1.26.11

Reaction

endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule =

Synonyms

(tRNase) Z, 3 tRNase, 3' tRNase, 3'-tRNA processing endoribonuclease, 3'-tRNase, AthTrz1, AthTrz2, AthTrz3, AthTrz4, BsuTrz, CelTrz, DmeTrz, EcoTrz, EcoZ, Elac, Elac1, ELAC2, HsaTrz1, HsaTrz2, HvoTrz, long form of 3' tRNase, long form of tRNA 3' processing endoribonuclease, long form of tRNase Z, MjaTrz, nuclease, transfer ribonucleate maturation 3'-endoribo-(9CI), PaeTrz, pre-tRNA processing endoribonuclease, precursor tRNA 3'-end processing endoribonuclease, ribonuclease Z, RNase BN, RNase Z, RNase ZL, RNase ZS1, RNaseZ, RNZ, SceTrz, SpTrz1p, SpTrz2p, TM0207, TmaTrz, TMS5 protein, transfer RNA maturation endonuclease, tRNA 3 endonuclease, tRNA 3' processing endoribonuclease, tRNA 3'-processing enzyme tRNase Z, tRNA precursor-processing endoribonuclease, tRNase Z, tRNase Z2, tRNase ZL, tRNase ZS, tRNaseZ, tRnaseZL, tRnaseZS, Trz, TRZ1, Trz1p, TRZ2, TrZL1, TrZL2, TrZS1, TrZS2, YP_145327, YqiK, YqjK, zinc phosphodiesterase, zinc-dependent phosphodiesterase, ZiPD

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.11 tRNase Z

Crystallization

Crystallization on EC 3.1.26.11 - tRNase Z

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization with tRNAThr
crystal structure of different tRNase Z enzymes with regard to canonical sequence motifs reviewed, overview about substrate recognition and cleavage sites of tRNase Z given
-
the enzyme bears significant similarity to Zn-dependent metallo-beta-lactamases, two Zn2+ in the active site are complexed by H63, H65, D67, H68, H140, D211 and H269
-
the enzyme forms a homodimer, the monomeric subunits are arranged in head-to-head fashion. The monomers concertedly build an active site cleft which is capable of accommodating single-stranded RNA
-
crystal structure of different tRNase Z enzymes with regard to canonical sequence motifs reviewed, overview about substrate recognition and cleavage sites of tRNase Z given
-
each monomer exhibits the typical metallo-beta-lactamase fold, 2 Zn2+ ions are complexed at the active site
-
structural features summarized
-
structures of free and RNA-bound prokaryotic tRNase Z proteins compared, overview, electrostatic surface representation, catalytic site and cleavage mechanism indicated, overview
-
the enzyme forms a homodimer, the monomeric subunits are arranged in head-to-head fashion. The monomers concertedly build an active site cleft which is capable of accommodating single-stranded RNA
-
structural features of tRNase Z summarized, overview
-
sitting drop vapor diffusion method at 18°C, 3.1 A crystal structure
four-layer alpha-beta/beta-alpha sandwich fold determined
-
structure of flexible arm and the zinc-bound active site determined, 1.97 A resolution, hanging-drop procedure, data collection and refinement statistics shown, flexible arm distinct from other bacterial enzymes, differences in dimer orientation probably due to unique cleavage-site specificity
-
the enzyme forms a homodimer, the monomeric subunits are arranged in head-to-head fashion. The monomers concertedly build an active site cleft which is capable of accommodating single-stranded RNA
-