1i97
From Proteopedia
(New page: 200px<br /><applet load="1i97" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i97, resolution 4.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1i97.gif|left|200px]]<br /><applet load="1i97" size=" | + | [[Image:1i97.gif|left|200px]]<br /><applet load="1i97" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i97, resolution 4.5Å" /> | caption="1i97, resolution 4.5Å" /> | ||
'''CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS IN COMPLEX WITH TETRACYCLINE'''<br /> | '''CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS IN COMPLEX WITH TETRACYCLINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The small ribosomal subunit is responsible for the decoding of genetic | + | The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X-ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A-site inhibitor tetracycline, the universal initiation inhibitor edeine and the C-terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A-site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P-site tRNA. The location of the C-terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti-association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. |
==About this Structure== | ==About this Structure== | ||
| - | 1I97 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with MG, ZN, WO2 and TAC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1I97 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=WO2:'>WO2</scene> and <scene name='pdbligand=TAC:'>TAC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I97 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tetracycline]] | [[Category: tetracycline]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:19 2008'' |
Revision as of 11:09, 21 February 2008
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CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS IN COMPLEX WITH TETRACYCLINE
Overview
The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X-ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A-site inhibitor tetracycline, the universal initiation inhibitor edeine and the C-terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A-site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P-site tRNA. The location of the C-terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti-association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit.
About this Structure
1I97 is a Protein complex structure of sequences from Thermus thermophilus with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3., Pioletti M, Schlunzen F, Harms J, Zarivach R, Gluhmann M, Avila H, Bashan A, Bartels H, Auerbach T, Jacobi C, Hartsch T, Yonath A, Franceschi F, EMBO J. 2001 Apr 17;20(8):1829-39. PMID:11296217
Page seeded by OCA on Thu Feb 21 13:09:19 2008
Categories: Protein complex | Thermus thermophilus | Avila, H. | Bartels, H. | Franceschi, F. | Gluehmann, M. | Harms, J. | Hartsch, T. | Jacobi, C. | Pioletti, M. | Schluenzen, F. | Yonath, A. | Zarivach, R. | MG | TAC | WO2 | ZN | 30s ribosome | Antibiotics | Tetracycline
