Sandbox Reserved 1263
From Proteopedia
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==Lambda Repressor-Operator Complex == | ==Lambda Repressor-Operator Complex == | ||
<StructureSection load='1lmb' size='340' side='r> | <StructureSection load='1lmb' size='340' side='r> | ||
| - | The repressor molecule consists of a bacteriophage's <scene name='75/751156/Double_stranded_dna/2'>double stranded DNA</scene> and two <scene name='75/751156/Two_arm/1'>terminal arms</scene>, creating a lambda repressor operator complex. The <scene name='75/751156/Operator_site_at_one_arm/1'> operator site at each arm</scene> interacts with the bacteriophage DNA. | ||
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== Structure == | == Structure == | ||
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| + | The complex is composed of a lambda repressor homodimer and bacteriophage DNA. A bacteriophage has <scene name='75/751156/Double_stranded_dna/2'>double stranded DNA</scene>. The repressor molecule has two of the same <scene name='75/751156/Two_arm/1'>terminal arms</scene>, polypeptide chains made from 236 amino acids. These two arms/chains interact with bacteriophage DNA by binding to an <scene name='75/751156/Operator_site_at_one_arm/1'>operator site</scene> on the DNA. | ||
== Function == | == Function == | ||
| - | + | The repressor molecule, two dimers, stops lysing of infected cell. | |
== Structural highlights == | == Structural highlights == | ||
Revision as of 20:41, 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
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