Sandbox Reserved 1263
From Proteopedia
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{{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Lambda Repressor-Operator Complex == | ==Lambda Repressor-Operator Complex == | ||
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| + | The lambda repressor operator complex is a 4 chain structure with two arms each containing two of the chains. The structure of this protein allows it to enter the host bacterias’ chromosome and stay inactive. This position of the protein stops the transcription of the proteins necessary for lytic development of the phage Lambda. Specifically, the lambda repressor contains the DNA binding domain; an area of the larger structure plays a role in binding to the DNA. The Lambda Repressor is composed of 2 domains, the C-terminal domain (CTD) and N-terminal domain (NTD), and a connecting region that connects the CTD and the NTD. The interactions between the CTD and NTD create a homodimer in the protein. | ||
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<StructureSection load='1lmb' size='340' side='r> | <StructureSection load='1lmb' size='340' side='r> | ||
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== Structure == | == Structure == | ||
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== Function == | == Function == | ||
| - | The repressor molecule, two dimers, stops lysing of infected cell. | + | The repressor molecule, two dimers, stops lysing of the infected cell. In the phage lambda, the repressor is the Cl protein. In order to repress, the two dimers bind to adjacent sites on the DNA. When they bind together, the Cro gene is repressed, and the Cl (repression) genes are activated. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 20:52, 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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Lambda Repressor-Operator Complex
The lambda repressor operator complex is a 4 chain structure with two arms each containing two of the chains. The structure of this protein allows it to enter the host bacterias’ chromosome and stay inactive. This position of the protein stops the transcription of the proteins necessary for lytic development of the phage Lambda. Specifically, the lambda repressor contains the DNA binding domain; an area of the larger structure plays a role in binding to the DNA. The Lambda Repressor is composed of 2 domains, the C-terminal domain (CTD) and N-terminal domain (NTD), and a connecting region that connects the CTD and the NTD. The interactions between the CTD and NTD create a homodimer in the protein.
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