Sandbox Reserved 1269
From Proteopedia
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| - | {{Sandbox_Reserved_O'Brochta_HLSC322}} | + | {{Sandbox_Reserved_O'Brochta_HLSC322}} |
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == Function == | + | ==iYSA== |
| + | ==Function of 1YSA== | ||
| + | 1YSA is a transcription factor that activates over 30 genes necessary for amino acid or purine biosynthesis. iYSA binds to the DNA sequence: 5'-TGA[CG]TCA-3'. | ||
| + | ==Structure, Interactions, and Location== | ||
| + | 1YSA is a four-chain structure. It interacts with DNA and binds DNA as a dimer. 1YSA interacts in several locations within the DNA. Additionally, 1YSA interacts with the protein Gcn4. Within DNA, 1YSA binds to DNA (5'-3 D(*tp*tp*cp*cp*tp*ap*tp*gp*ap*cp*tp*cp*ap*tp*cp*cp*a4 P*gp*tp*t)-3') and DNA (5'-9 D(*ap*ap*ap*cp*tp*gp*gp*ap*tp*gp*ap*gp*tp*cp*ap*tp*a10 P*gp*gp*a)-3'). The location of 1YSA within a cell is in nucleus P03069. | ||
| + | ==Origin== | ||
| + | 1YSA originates from the organism ''Saccharomyces cerevisiae'', or commonly known as baker's yeast. | ||
| - | == Disease == | ||
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| - | == Relevance == | ||
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| - | == Structural highlights == | ||
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| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
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| - | </StructureSection> | ||
| - | == References == | ||
| - | <references/> | ||
| + | ==References== | ||
| + | www.proteopedia.org/wiki/index.php/1ysa | ||
| + | www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=1ysa | ||
| + | www.pdbj.org/mine/summary/1ysa | ||
| + | www.uniprot.org/uniprot/P03069 | ||
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| - | + | 1ysa | |
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Revision as of 20:26, 8 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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