1i6v
From Proteopedia
(New page: 200px<br /><applet load="1i6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6v, resolution 3.3Å" /> '''THERMUS AQUATICUS COR...) |
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| - | [[Image:1i6v.gif|left|200px]]<br /><applet load="1i6v" size=" | + | [[Image:1i6v.gif|left|200px]]<br /><applet load="1i6v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i6v, resolution 3.3Å" /> | caption="1i6v, resolution 3.3Å" /> | ||
'''THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX'''<br /> | '''THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics | + | Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics against bacterial pathogens and is a key component of anti-tuberculosis therapy, stemming from its inhibition of the bacterial RNA polymerase (RNAP). We determined the crystal structure of Thermus aquaticus core RNAP complexed with Rif. The inhibitor binds in a pocket of the RNAP beta subunit deep within the DNA/RNA channel, but more than 12 A away from the active site. The structure, combined with biochemical results, explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length. |
==About this Structure== | ==About this Structure== | ||
| - | 1I6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG, ZN and RFP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http:// | + | 1I6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=RFP:'>RFP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
| - | [[Category: Campbell, E | + | [[Category: Campbell, E A.]] |
| - | [[Category: Darst, S | + | [[Category: Darst, S A.]] |
[[Category: Goldfarb, A.]] | [[Category: Goldfarb, A.]] | ||
[[Category: Korzheva, N.]] | [[Category: Korzheva, N.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:33 2008'' |
Revision as of 11:08, 21 February 2008
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THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX
Overview
Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics against bacterial pathogens and is a key component of anti-tuberculosis therapy, stemming from its inhibition of the bacterial RNA polymerase (RNAP). We determined the crystal structure of Thermus aquaticus core RNAP complexed with Rif. The inhibitor binds in a pocket of the RNAP beta subunit deep within the DNA/RNA channel, but more than 12 A away from the active site. The structure, combined with biochemical results, explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.
About this Structure
1I6V is a Protein complex structure of sequences from Thermus aquaticus with , and as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
Reference
Structural mechanism for rifampicin inhibition of bacterial rna polymerase., Campbell EA, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, Darst SA, Cell. 2001 Mar 23;104(6):901-12. PMID:11290327
Page seeded by OCA on Thu Feb 21 13:08:33 2008
