Crystallization (Comment) | Organism |
---|---|
structure of CsdA_218-445 is determined by X-ray diffraction and refined to an R factor of 0.225, with an Rfree of 0.268 at a resolution of 2.3 A by molecular replacement using Hera (PDB ID 3EAQ) as the model. The structure of CsdA_218-445 includes two RecA-like domains (RecA2) and two DDs, which form a V-shape dimer. The V-shape conformation of the CsdA_218-445 dimer in solution is further confirmed by SAXS experiments. Conformational flexibilities of CsdA_1-445 and CsdA_FL are revealed by SAXS | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Escherichia coli | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A9P6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Escherichia coli | ADP + phosphate | - |
? | |
additional information | analysis of ATPase and unwinding activities of CsdA_564 and CsdA_1-445, and of RNA-binding properties of the C-terminal regions of CsdA and CsdA_RNA-binding domain, overview | Escherichia coli | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | the helicase core of CsdA is comprised of two RecA-like domains (RecA1 and RecA2) joined by a flexible linker and contains all conserved motifs, two previously auxiliary domains are found: a dimerization domain (DD) and an RNA-binding domain (RBD), conformational flexibilities of the helicase core domains and C-terminal regions, enzyme domain structure, three-dimensional modelling, detailed overview. DD is indispensable for stabilizing the CsdA dimeric structure. Structure comparisons | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ATP-dependent RNA helicase | - |
Escherichia coli |
cold-shock DEAD-box protein A | - |
Escherichia coli |
CsdA | - |
Escherichia coli |
DeaD | - |
Escherichia coli |
DEAD-box RNA helicase | - |
Escherichia coli |
RNA helicase CsdA | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | DEAD-box proteins belong to a ubiquitous family of RNA helicases, which are widely found from prokaryotes to eukaryotes and participate in multiple cellular processes, such as premRNA splicing, translation initiation, modulating RNA-protein complexes, RNA decay, and ribosome biogenesis. Sequence alignment and architecture of different DEAD-Box proteins, overview | Escherichia coli |
additional information | the long, flexible C-terminal regions of CsdA are essential for high enzymatic activity and strong RNA-binding affinity, and the RNA-binding domain prefers binding single-stranded G-rich RNA. CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD can specifically bind to the regions with a preference for single-stranded G-rich RNA, which may help to bring the helicase core to unwind the adjacent duplex, structure of dimeric RNA helicase CsdA and indispensable role of its C-terminal regions, overview | Escherichia coli |