Sandbox Reserved 1298
From Proteopedia
m |
|||
| Line 2: | Line 2: | ||
==Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme== | ==Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme== | ||
| - | <Structure load='4yg2' size='350' frame='true' align='right' caption=' | + | <Structure load='4yg2' size='350' frame='true' align='right' caption='RNA Polymerase' scene='Insert optional scene name here' /> |
| - | + | == Functions!!!!!!!!!!!!!!!!!!!!!!!!Lawl XD == | |
| - | == | + | |
| + | == What it interacts == | ||
| + | |||
| + | == Interaction (Where, When, How, Why, End My Suffering) == | ||
| + | |||
| + | == Is it from Kenya?? Where's the Birth Certificate == | ||
| + | E. Coli, so I guess | ||
== Disease == | == Disease == | ||
| - | + | E.coli use it, so I guess salmonella. | |
== Relevance == | == Relevance == | ||
| - | + | It's lit G. | |
== Structural highlights == | == Structural highlights == | ||
| - | + | Check ESPN, my guy | |
| - | + | == Fun Fax, b == | |
| + | Most studied bacterial RNA polymerase. | ||
| + | The Donald's favorite bacterial RNA polymerase. | ||
</StructureSection> | </StructureSection> | ||
| - | == References == | ||
| - | <references/> | ||
Revision as of 21:30, 9 February 2017
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.
| |||||||||||
Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme
|
Functions!!!!!!!!!!!!!!!!!!!!!!!!Lawl XD
What it interacts
Interaction (Where, When, How, Why, End My Suffering)
Is it from Kenya?? Where's the Birth Certificate
E. Coli, so I guess
Disease
E.coli use it, so I guess salmonella.
Relevance
It's lit G.
Structural highlights
Check ESPN, my guy
Fun Fax, b
Most studied bacterial RNA polymerase. The Donald's favorite bacterial RNA polymerase.
</StructureSection>
