Sandbox Reserved 1258
From Proteopedia
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<StructureSection load='1j1v' size='340' side='right' caption='DNA.' scene=''> | <StructureSection load='1j1v' size='340' side='right' caption='DNA.' scene=''> | ||
| - | <scene name='75/751151/Area_of_interaction/1'>area of interaction with DNA</scene> | ||
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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. 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. | 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. 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. | ||
| - | == Disease == | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
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The unique protein chain, chromosomal replication initiator protein dnaA (gene name: dnaA b3702 JW3679), assists in the regulation and regulation of chromosomal replication. Its function is ATP dependent, so it is only able to assist in replication once per cell cycle. | The unique protein chain, chromosomal replication initiator protein dnaA (gene name: dnaA b3702 JW3679), assists in the regulation and regulation of chromosomal replication. Its function is ATP dependent, so it is only able to assist in replication once per cell cycle. | ||
| + | <scene name='75/751151/Area_of_interaction/1'>area of interaction with DNA</scene> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 21:26, 7 February 2017
Contents |
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.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
