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From Proteopedia

1 genetics is ok
2 'Molecules it Interacts With and where '
3 'Origin'
4 'Structure'
5 'Molecules it Interacts With and where '
6 'Origin'
7 'Structure'
8 'Function"
9 References

genetics is ok

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER

PHENYLALANINE MAGNESIUM ION

'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.

'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.

Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.

which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER

PHENYLALANINE MAGNESIUM ION

'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.

'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.

Specific are highlighted here.

which play a crucial role in binding to the ribosome during translation.

'Function"

The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.

DnaA

DnaA is found in E. Coli. It plays a role in the initiation DNA replication by promoting the unwinding of DNA at the origin of replication (oriC). The activation of the initiation phase of DNA replication is based on the concentration of DnaA built up in the system. Initially, when a cell first divides, there isn't much DnaA in the system. As the cell grows, the amount of DnaA accumulates, eventually reaching a concentration that will trigger the initiation phase of DNA replication to begin. These are the of the DnaA.

Function

1J1V is a DnaA found in E. Coli that plays a role in the replication of DNA. Specifically, it is involved in the initiation of DNA replication by promoting the formation of the DNA Polymerase III holoenzyme at the origin of replication. This is accomplished as the DnaA binds to a specific consensus sequence known as the DnaA box sequence which can be found upstream of the origin of replication. The DnaA protein recognizes these sequences, for which it has a high affinity, and binds to the major groove; as a result of the binding, DNA bends 28 degrees. Interestingly enough, the DnaA box sequences that are much further upstream are what the protein shows greater affinity for, rather than those that are relatively close to the origin of replication. After the DnaA proteins bind to the DnaA box, the formation of the DNA Polymerase III subunits into the holoenzyme at the origin of replication is initiated.

Structural highlights

DnaA consists of two sections. It has (which is 94 amino acids long) and (which are 13 nucleotides long). The unique protein chain, chromosomal replication initiator protein dnaA (gene name: dnaA b3702 JW3679), assists in the regulation of chromosomal replication. Its function is ATP dependent, so it is only able to assist in replication once per cell cycle. However, ATP hydrolysis is only needed once to activate DnaA to bind with the oriC. After that, ATP is not needed for the creation of the oriC/DnaA complex and DNA unwinding.