Sandbox Reserved 1256
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 --> | ||
| - | == | + | ==Structure== |
| - | + | 1AIS is a TATA Box binding protein (TBP) within archaea basal transcriptional apparatus, located within the Hyperthermophile Pyrococcus Woesei. The TBP and basal transcriptional apparatus are used in the initiation of transcription within the cell's nucleus. The TBP is an asymmetric protein with <scene name='75/751149/Color_coded_tbp/1'>two unique protein chains and two unique nucleic acid chains</scene> (This model shows the TBP in red and the TATA box (DNA) in blue). 1AIS consists of the TBP, the transcription factor IIB homolog, and a DNA target (the TATA box). This transcriptional apparatus is similar to Eukaryotic, but is more symmetrical. | |
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| - | <Structure load=' | + | This TBP binds to the <scene name='75/751149/Ribbion_tbp/1'>minor groove</scene> of the TATA box in the core promotor of a gene (This model shows the close association of the protein and DNA.. THe TBP bends the DNA and partially unwinds it. The <scene name='75/751149/Space_filling_tbp/1'>structure</scene> of the TBP allows it to locate and bind to the TATA consensus sequence (This model also shows the two protein subunits of TBP in green and blue. The provides a less cluttered view of the structure of TBP, and makes it more clear that the TBP binds to the minor groove on the DNA and not the major groove). |
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| + | <Structure load='1ais' size='350' frame='true' align='right' caption='TATA Binding Protein'/> | ||
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
| - | == Structural highlights == | ||
| - | 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. | ||
| - | </StructureSection> | ||
== References == | == References == | ||
| - | + | [[1ais]] | |
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| + | Kosa, P. F., Ghosh, G., DeDecker, B. S., & Sigler, P. B. (1997). The 2.1-Å crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box. Proceedings of the National Academy of Sciences of the United States of America, 94(12), 6042–6047. | ||
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| + | Pierce, B. A. (2012). Genetics: A Conceptual Approach. W.H. Freeman, 4th edition, 365-367. | ||
Current revision
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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Structure
1AIS is a TATA Box binding protein (TBP) within archaea basal transcriptional apparatus, located within the Hyperthermophile Pyrococcus Woesei. The TBP and basal transcriptional apparatus are used in the initiation of transcription within the cell's nucleus. The TBP is an asymmetric protein with (This model shows the TBP in red and the TATA box (DNA) in blue). 1AIS consists of the TBP, the transcription factor IIB homolog, and a DNA target (the TATA box). This transcriptional apparatus is similar to Eukaryotic, but is more symmetrical.
This TBP binds to the of the TATA box in the core promotor of a gene (This model shows the close association of the protein and DNA.. THe TBP bends the DNA and partially unwinds it. The of the TBP allows it to locate and bind to the TATA consensus sequence (This model also shows the two protein subunits of TBP in green and blue. The provides a less cluttered view of the structure of TBP, and makes it more clear that the TBP binds to the minor groove on the DNA and not the major groove).
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Function
Disease
Relevance
References
Kosa, P. F., Ghosh, G., DeDecker, B. S., & Sigler, P. B. (1997). The 2.1-Å crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box. Proceedings of the National Academy of Sciences of the United States of America, 94(12), 6042–6047.
Pierce, B. A. (2012). Genetics: A Conceptual Approach. W.H. Freeman, 4th edition, 365-367.
