User:Wayne Decatur/Sandbox Thermus 70S With Paromomycin
From Proteopedia
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The 70S is so large that the small paromomycin that is bound is not readily obvious, and so <scene name='User:Wayne_Decatur/Sandbox_Thermus_70S_With_Paromomycin/70swithparbest/6'>here the view zooms in and highlights paromomycin by making the ribosome partially translucent</scene>.   | The 70S is so large that the small paromomycin that is bound is not readily obvious, and so <scene name='User:Wayne_Decatur/Sandbox_Thermus_70S_With_Paromomycin/70swithparbest/6'>here the view zooms in and highlights paromomycin by making the ribosome partially translucent</scene>.   | ||
| - | Returning to  <scene name='User:Wayne_Decatur/Sandbox_Thermus_70S_With_Paromomycin/70swithpar/1'>the initial scene of the full ribosome</scene> now aware of the locale where paromomycinin is bound, it is clear that in the Thermus 70S paromomycin is observed binding to the penultimate helix of the small subunit (helix 44) at the decoding center where the anticodon stem loop of the tRNA contacts the mRNA.    | + | Returning to  <scene name='User:Wayne_Decatur/Sandbox_Thermus_70S_With_Paromomycin/70swithpar/1'>the initial scene of the full ribosome</scene> now aware of the locale where paromomycinin is bound, it is clear that in the Thermus 70S paromomycin is observed binding to the penultimate helix of the small subunit (helix 44) at the decoding center where the anticodon stem-loop of the <font color = 'pink'>A-site tRNA </font> contacts the mRNA (shown as yellow).    | 
<!--After much work, finally got 5S to go transparent by turning off cartoon and making it trace. Others seemed fine with cartoon. See   | <!--After much work, finally got 5S to go transparent by turning off cartoon and making it trace. Others seemed fine with cartoon. See   | ||
<scene name='User:Wayne_Decatur/Sandbox_Thermus_70S_With_Paromomycin/70swithparbest/3'>TextToBeDisplayed</scene>  | <scene name='User:Wayne_Decatur/Sandbox_Thermus_70S_With_Paromomycin/70swithparbest/3'>TextToBeDisplayed</scene>  | ||
Revision as of 04:29, 10 January 2010
Ribosome interactions with Paromomycin
Contents | 
Mechanism of action
 
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NEED TO DO STILL: SSU alone with PAR
Ramakrishnan one with Par
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The 70S is so large that the small paromomycin that is bound is not readily obvious, and so .
Returning to now aware of the locale where paromomycinin is bound, it is clear that in the Thermus 70S paromomycin is observed binding to the penultimate helix of the small subunit (helix 44) at the decoding center where the anticodon stem-loop of the A-site tRNA contacts the mRNA (shown as yellow).
Add the e. coli 70S that has two molecules bound
About these Structure
2j00 is a 25 chains structure of sequences from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.
2j01 is a 31 chains structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA. Versions of 2j00 and 2j01 optimized for use online as described here are used on this page. You may wish to examine the ADD LINK basics of the subunit.
Reference for the Structures
- Selmer M, Dunham CM, Murphy FV 4th, Weixlbaumer A, Petry S, Kelley AC, Weir JR, Ramakrishnan V. Structure of the 70S ribosome complexed with mRNA and tRNA. Science. 2006 Sep 29;313(5795):1935-42. Epub 2006 Sep 7. PMID:16959973
 
Related Structures
References
- ↑ Ogle JM, Carter AP, Ramakrishnan V. Insights into the decoding mechanism from recent ribosome structures. Trends Biochem Sci. 2003 May;28(5):259-66. PMID:12765838
 
Additional Literature and Resources
- Auerbach T, Bashan A, Yonath A. Ribosomal antibiotics: structural basis for resistance, synergism and selectivity. Trends Biotechnol. 2004 Nov;22(11):570-6. PMID:15491801 doi:10.1016/j.tibtech.2004.09.006
 
Categories: Escherichia coli | Thermus thermophilus | Dunham, C M. | Kelley, A C. | Murphy, F V. | Petry, S. | Ramakrishnan, V. | Selmer, M. | Weir, J R. | Weixlbaumer, A. | Mrna | Paromomycin | Ribosome | Translation | Trna | Antibiotic | 50S | 30S | 70S | Large ribosomal subunit
