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Interaction information
Interaction summary
Short label
tRNA delta(2)-isopentenylpyrophosphate transferase-tRNA(Phe)
Full name
tRNA delta(2)-isopentenylpyrophosphate transferase interacts with tRNA(Phe)
Source database
RCSB PDB
ID
2ZXU
Date modified
2011-03-25 19:16:14 JST
Protein information
Short label
tRNA delta(2)-isopentenylpyrophosphate transferase
Full name
Chain A,B of model 2ZXU: tRNA delta(2)-isopentenylpyrophosphate transferase
Gene
miaA (delta(2)-isopentenylpyrophosphate tRNA-adenosine transferase)
GeneID
948690
Official symbol
miaA
Synonyms
3 synonym(s)
Description
delta(2)-isopentenylpyrophosphate tRNA-adenosine transferase
Ontologies
2 ontology(s)
Functions
0 function(s)
Processes
1 process(s)
GO:0009451
RNA modification
Evidence
n/a
Term ID
GO:0009451
Name
RNA modification
Namespace
biological_process
Definition
The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically." [GOC:go_curators, ISBN:1555811337 "Modification and Editing of RNA
Synonyms
1 synonym(s)
Is-a
2 item(s)
GO:0016070
RNA metabolic process
GO:0043412
macromolecule modification
Components
1 component(s)
GO:0005737
cytoplasm
Evidence
n/a
Term ID
GO:0005737
Name
cytoplasm
Namespace
cellular_component
Definition
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
Is-a
1 item(s)
GO:0044424
intracellular part
Origin
Escherichia coli K-12
NCBI Taxonomy ID
83333
Name
Escherichia coli K-12
Synonyms
1 synonym(s).
Cross references
1 item(s)
UniProt
P16384
Sequence
2ZXUA:tRNA delta(2)-isopentenylpyrophosphate transferase
RNA information
Short label
tRNA(Phe)
Full name
Chain C,D of model 2ZXU: tRNA(Phe)
Gene
gspM (general secretory pathway component, cryptic)
GeneID
6058075
Official symbol
gspM
Description
general secretory pathway component, cryptic
Cross references
1 item(s)
GenBank Nucleotide
169887498
Sequence
2ZXUC:tRNA(Phe)
Experiments (1)
Experiment 1
chimnaronk-2009
Full name
X-ray diffraction
Detection method
x-ray crystallography (MI:0114)
Term ID
MI:0114
Name
x-ray crystallography
Definition
Analysis of a diffraction pattern generated by a single crystal. X-rays have a wavelength, typically around 1 Angstrom (the diameter of a hydrogen atom). If a narrow parallel beam of X-rays is directed at a sample of a pure protein, most of the X-rays will pass straight through it. A small fraction, however, will be scattered by the atoms in the sample. If the sample is a well-ordered crystal, the scattered waves will reinforce one another at certain points and will appear as diffraction spots when the X-rays are recorded by a suitable detector. The position and intensity of each spot in the X-ray diffraction pattern contain information about the position and nature of the atoms in the crystal. The three-dimensional structure of a large molecule can be deduced from the electron-density map of its crystal. In recent years X-ray diffraction analysis has become increasingly automated, and now the slowest step is likely to be the production of suitable macromolecule crystals. This requires high concentration of very pure macromolecule and empirical searching for the proper crystallisation conditions.
Synonyms
2 synonym(s)
X-ray (PSI-MI-alternate)
x-ray diffraction (PSI-MI-short)
Is-a
2 item(s)
MI:0013
biophysical
MI:0659
experimental feature detection
Host organisms
1 host organism(s)
Origin
Escherichia coli
NCBI Taxonomy ID
562
Name
Escherichia coli
Synonyms
16 synonym(s).
"Bacillus coli" Migula 1895
"Bacterium coli commune" Escherich 1885
"Bacterium coli" (Migula 1895) Lehmann and Neumann 1896
Bacillus coli
Bacterium coli
Bacterium coli commune
Enterococcus coli
Escherchia coli
Escherichia coli (Migula 1895) Castellani and Chalmers 1919
Escherichia coli retron Ec107
Escherichia coli retron Ec67
Escherichia coli retron Ec79
Escherichia coli retron Ec86
Eschericia coli
bacterium 10a
bacterium E3
Reference
CHIMNARONK, Sarin, et al. , Biochemistry 2009 Jun;48(23):5057-65
PMID
19435325
Title
Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon.
Authors
CHIMNARONK, Sarin, et al.
CHIMNARONK, Sarin
FOROUHAR, Farhad
SAKAI, Junichi
YAO, Min
TRON, Cecile M
ATTA, Mohamed
FONTECAVE, Marc
HUNT, John F
TANAKA, Isao
Citation
Biochemistry 2009 Jun;48(23):5057-65
References (1)
Reference 1
CHIMNARONK, Sarin, et al. , Biochemistry 2009 Jun;48(23):5057-65
PMID
19435325
Title
Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon.
Authors
CHIMNARONK, Sarin, et al.
CHIMNARONK, Sarin
FOROUHAR, Farhad
SAKAI, Junichi
YAO, Min
TRON, Cecile M
ATTA, Mohamed
FONTECAVE, Marc
HUNT, John F
TANAKA, Isao
Citation
Biochemistry 2009 Jun;48(23):5057-65
Related articles (1)
Article 1
CHIMNARONK, Sarin, et al. , Biochemistry 2009 Jun;48(23):5057-65
PMID
19435325
Title
Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon.
Authors
CHIMNARONK, Sarin, et al.
CHIMNARONK, Sarin
FOROUHAR, Farhad
SAKAI, Junichi
YAO, Min
TRON, Cecile M
ATTA, Mohamed
FONTECAVE, Marc
HUNT, John F
TANAKA, Isao
Citation
Biochemistry 2009 Jun;48(23):5057-65
Attributes (3)
Attributes
3 attribute(s)
3d-structure
Crystal structure of tRNA modification enzyme MiaA in the complex with tRNA(Phe) and DMASPP
3d-resolution
2.75A
3d-r-factors
working 23.700%, free 28.100%