Reverse transcriptase: Difference between revisions
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<applet size='[450,338]' frame='true' align='right' name='Reverse Transcriptase scene='Reverse_transcriptase/Presentation/3' caption='The hand-like two-enzymes-in-one protein that amazingly makes DNA from RNA' /> | <applet size='[450,338]' frame='true' align='right' name='Reverse Transcriptase scene='Reverse_transcriptase/Presentation/3' caption='The hand-like two-enzymes-in-one protein that amazingly makes DNA from RNA' /> | ||
This ''hand-like'' <scene name='Reverse_transcriptase/Chains/2'>heterodimer</scene> protein has an usual length of 1000 residues (560 in Chain A and 440 for B), a third of them involved in alpha helices and almost a quarter involved in beta sheets, showing α+β <scene name='Reverse_transcriptase/Secondary/2'>secondary structure</scene> domains. <scene name='Reverse_transcriptase/Chaina/2'>Chain A</scene> has an usual weight of 66KDa whereas <scene name='Reverse_transcriptase/Chainb/2'>Chain B</scene> is around 51KDa. These monomers are derived from the same gene, but p51 lacks the amino acids of one active site and has a different tertiary structure conformation compared to p66. Because of this, p51 is enzymatically inactive. <ref>PMID: 1377403</ref> <!-- [http://www.sciencemag.org.silk.library.umass.edu:2048/cgi/content/abstract/sci;256/5065/1783?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&andorexacttitleabs=and&andorexactfulltext=and&searchid=1&FIRSTINDEX=0&volume=256&firstpage=1783&resourcetype=HWCIT] --> | This ''hand-like'' <scene name='Reverse_transcriptase/Chains/2'>heterodimer</scene> protein has an usual length of 1000 residues (560 in Chain A and 440 for B), a third of them involved in alpha helices and almost a quarter involved in beta sheets, showing α+β <scene name='Reverse_transcriptase/Secondary/2'>secondary structure</scene> domains. <scene name='Reverse_transcriptase/Chaina/2'>Chain A</scene> has an usual weight of 66KDa whereas <scene name='Reverse_transcriptase/Chainb/2'>Chain B</scene> is around 51KDa. These monomers are derived from the same gene, but p51 lacks the amino acids of one active site and has a different tertiary structure conformation compared to p66. Because of this, p51 is enzymatically inactive. <ref>PMID: 1377403</ref> <!-- [http://www.sciencemag.org.silk.library.umass.edu:2048/cgi/content/abstract/sci;256/5065/1783?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&andorexacttitleabs=and&andorexactfulltext=and&searchid=1&FIRSTINDEX=0&volume=256&firstpage=1783&resourcetype=HWCIT] --> | ||
There are five distinct structures within the p66 subchain that are used to describe the functions of RT: the fingers (residues 1–85 and 118–155), the palm (residues 86–117 and 156–236), the thumb (residues 237–318), the connection (319–426), and the RNase H (residues 427-end).[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2881421/?tool=pubmed] | There are five distinct structures within the p66 subchain that are used to describe the functions of RT: the fingers (residues 1–85 and 118–155), the palm (residues 86–117 and 156–236), the thumb (residues 237–318), the connection (319–426), and the RNase H (residues 427-end). The palm contains the main active site (residues 110, 185-186).[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2881421/?tool=pubmed] | ||
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