Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.1.26.11 |
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
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.1.26.11 |
Zn2+ |
part of active site, Zn1 ccoordinated with tetrahedral geometry and Zn2 coordinated with trigonal bipyramidal geometry, determined by crystallization |
Thermotoga maritima |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.1.26.11 |
Thermotoga maritima |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.1.26.11 |
prior to crystallization |
Thermotoga maritima |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
3.1.26.11 |
cell culture |
- |
Thermotoga maritima |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.1.26.11 |
additional information |
tRNA 3'-processing endoribonuclease, member of the metallo-beta-lactamase superfamily |
Thermotoga maritima |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.1.26.11 |
dimer |
crystallization, active site located near the dimer interface, flexible arm clamping the tRNA protrudes from the core into solution |
Thermotoga maritima |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.1.26.11 |
tRNase Z |
- |
Thermotoga maritima |