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Literature summary for 3.1.26.11 extracted from

  • Ishii, R.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.; Yokoyama, S.
    The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes (2007), Acta Crystallogr. Sect. F, 63, 637-641.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.11

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Thermotoga maritima

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ part of active site, Zn1 ccoordinated with tetrahedral geometry and Zn2 coordinated with trigonal bipyramidal geometry, determined by crystallization Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Purification (Commentary)

Purification (Comment) Organism
prior to crystallization Thermotoga maritima

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
 Thermotoga maritima
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information tRNA 3'-processing endoribonuclease, member of the metallo-beta-lactamase superfamily Thermotoga maritima ?
-
 ?

Subunits

Subunits Comment Organism
dimer crystallization, active site located near the dimer interface, flexible arm clamping the tRNA protrudes from the core into solution Thermotoga maritima

Synonyms

Synonyms Comment Organism
tRNase Z
-
 Thermotoga maritima