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Literature summary for 3.6.5.3 extracted from

  • Kumar, V.; Chen, Y.; Ero, R.; Ahmed, T.; Tan, J.; Li, Z.; Wong, A.S.; Bhushan, S.; Gao, Y.G.
    Structure of BipA in GTP form bound to the ratcheted ribosome (2015), Proc. Natl. Acad. Sci. USA, 112, 10944-10949 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.3

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-form, and GDP- and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA, X-ray diffraction structure determination and analysis Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
ribosome determination of the structure of BipA in GTP form bound to the ratcheted ribosome, modeling, detailed overview. Positioning of the C-terminal domain of BipA in ribosomal A site Escherichia coli 5840
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Escherichia coli
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0DTT0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?
additional information apo-form, and GDP- and nonhydrolysable GTP analogue guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA, structure analysis, overview Escherichia coli ?
-
-

Subunits

Subunits Comment Organism
More the C-terminal domain of BipA has a unique fold Escherichia coli

Synonyms

Synonyms Comment Organism
50S ribosomal subunit assembly factor UniProt Escherichia coli
BipA
-
 Escherichia coli
BPI-inducible protein A
-
 Escherichia coli

General Information

General Information Comment Organism
evolution BPI-inducible protein A (BipA) is a member of the family of ribosomedependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Comparison of domain arrangement and overall structure of EF-G, EF4, and BipA, overview Escherichia coli
additional information analysis of the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form at 4.7 A resolution, the unique structural attributes of BipA interactions with the ribosome and A-site tRNA function in regulating translation, translational factor recruitment and GTPase activation mechanisms by the ribosome, overview Escherichia coli
physiological function BPI-inducible protein A (BipA) is a GTPase involved in bacterial stress response. BipA is working as a ribosome-dependent translational GTPase factor and interacts with the A-site tRNA Escherichia coli