Sandbox Reserved 1391
From Proteopedia
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| - | </StructureSection>{{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
== Overview == | == Overview == | ||
| - | <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. | ||
| - | These are the <scene name='77/777711/Basic_parts_of_dna_polymerase/1'>basic parts of DNA Polymerase</scene> This next scene is the <scene name='77/777711/Secondary_structure/1'>Text To Be Displayed</scene> of DNA Polymerase III. The red/pink are alpha helixes and the yellow are beta pleated sheets. | ||
| + | <Structure load='4GX8' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></StructureSection>{{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| + | DNA polymerase 3 is the primary enzyme responsible for prokaryotic DNA replication. It was first discovered by Thomas Kornberg and Malcolm Gefter in 1970. This polymerase works in conjunction with four other polymerases. These include polymerase 1,2,4, and 5. | ||
== Function == | == Function == | ||
| - | <scene name='77/777711/Dna_polymerase_iii_helix/2'>This is the helix of the polymerase</scene> | ||
| - | DNA Polymerase III is an enzyme found in prokaryotes and it is responsible for DNA replication. It was discovered Thomas Kornberg and Malcolm Gefter in 1970. == | ||
| - | + | As mentioned DNA Polymerase 3 is responsible for replicating DNA in prokaryotes. It's activity starts after separation of strands at the origin of replication. The two most important subunits of this polymerase are the α subunit that links the nucleotides together via a phosphodiester bond and the ε subunit that ensures the bases are accurate via proofreading mechanisms. It can synthesize base pairs at a rate of about 1000 nucleotides per second and can only move in the 5' to 3' direction. One thing unique about this enzyme is the sliding clamp which is a donut shaped protein that allows the polymerase to bind to the DNA strands and move along it. | |
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== Structural highlights == | == Structural highlights == | ||
| + | This enzyme contains many different regions that all have different properties. These are the <scene name='77/777711/Hydrophobic_and_polar_regions/1'>hydrophobic and polar regions</scene> of the polymerase. The purple regions are towards the outside because they are polar and therefore hydrophilic. The gray regions are hydrophobic regions. This next scene shows the <scene name='77/777711/Secondary_structure/2'>secondary structure </scene> of the polymerase. This consists of alpha helices which are pink and beta pleated sheets which are yellow. These secondary structures form via hydrogen bonding between the amino acid backbones. Finally, another region we will talk about are the <scene name='77/777711/Basic_and_positive/1'>Basic and Positive </scene> regions of the polymerase. These regions are another example of the hydrophilic aspects of the proteins. All 3 of these and so many others that we did not talk about go to show the extreme complexity of this beautiful and indispensable enzyme. It's a shame we aren't prokaryotes! :( | ||
| - | 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 == | ||
| + | http://www.rcsb.org/structure/4GX8 | ||
| + | https://www.sciencedirect.com/topics/medicine-and-dentistry/dna-polymerase-iii-holoenzyme | ||
<references/> | <references/> | ||
Current revision
Contents |
Overview
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| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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DNA polymerase 3 is the primary enzyme responsible for prokaryotic DNA replication. It was first discovered by Thomas Kornberg and Malcolm Gefter in 1970. This polymerase works in conjunction with four other polymerases. These include polymerase 1,2,4, and 5.
Function
As mentioned DNA Polymerase 3 is responsible for replicating DNA in prokaryotes. It's activity starts after separation of strands at the origin of replication. The two most important subunits of this polymerase are the α subunit that links the nucleotides together via a phosphodiester bond and the ε subunit that ensures the bases are accurate via proofreading mechanisms. It can synthesize base pairs at a rate of about 1000 nucleotides per second and can only move in the 5' to 3' direction. One thing unique about this enzyme is the sliding clamp which is a donut shaped protein that allows the polymerase to bind to the DNA strands and move along it.
Structural highlights
This enzyme contains many different regions that all have different properties. These are the of the polymerase. The purple regions are towards the outside because they are polar and therefore hydrophilic. The gray regions are hydrophobic regions. This next scene shows the of the polymerase. This consists of alpha helices which are pink and beta pleated sheets which are yellow. These secondary structures form via hydrogen bonding between the amino acid backbones. Finally, another region we will talk about are the regions of the polymerase. These regions are another example of the hydrophilic aspects of the proteins. All 3 of these and so many others that we did not talk about go to show the extreme complexity of this beautiful and indispensable enzyme. It's a shame we aren't prokaryotes! :(
References
http://www.rcsb.org/structure/4GX8 https://www.sciencedirect.com/topics/medicine-and-dentistry/dna-polymerase-iii-holoenzyme
