1ynn

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[[Image:1ynn.gif|left|200px]]
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{{Seed}}
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[[Image:1ynn.png|left|200px]]
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{{STRUCTURE_1ynn| PDB=1ynn | SCENE= }}
{{STRUCTURE_1ynn| PDB=1ynn | SCENE= }}
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'''Taq RNA polymerase-rifampicin complex'''
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===Taq RNA polymerase-rifampicin complex===
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==Overview==
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A combined structural, functional, and genetic approach was used to investigate inhibition of bacterial RNA polymerase (RNAP) by sorangicin (Sor), a macrolide polyether antibiotic. Sor lacks chemical and structural similarity to the ansamycin rifampicin (Rif), an RNAP inhibitor widely used to treat tuberculosis. Nevertheless, structural analysis revealed Sor binds in the same RNAP beta subunit pocket as Rif, with almost complete overlap of RNAP binding determinants, and functional analysis revealed that both antibiotics inhibit transcription by directly blocking the path of the elongating transcript at a length of 2-3 nucleotides. Genetic analysis indicates that Rif binding is extremely sensitive to mutations expected to change the shape of the antibiotic binding pocket, while Sor is not. We suggest that conformational flexibility of Sor, in contrast to the rigid conformation of Rif, allows Sor to adapt to changes in the binding pocket. This has important implications for drug design against rapidly mutating targets.
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The line below this paragraph, {{ABSTRACT_PUBMED_15692574}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15692574 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15692574}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase., Campbell EA, Pavlova O, Zenkin N, Leon F, Irschik H, Jansen R, Severinov K, Darst SA, EMBO J. 2005 Feb 23;24(4):674-82. Epub 2005 Feb 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15692574 15692574]
Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase., Campbell EA, Pavlova O, Zenkin N, Leon F, Irschik H, Jansen R, Severinov K, Darst SA, EMBO J. 2005 Feb 23;24(4):674-82. Epub 2005 Feb 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15692574 15692574]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11290327 11290327]
[[Category: DNA-directed RNA polymerase]]
[[Category: DNA-directed RNA polymerase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Rna polymerase]]
[[Category: Rna polymerase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:33:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:49:32 2008''

Revision as of 14:49, 28 July 2008

Image:1ynn.png

Template:STRUCTURE 1ynn

Taq RNA polymerase-rifampicin complex

Template:ABSTRACT PUBMED 15692574

About this Structure

1YNN is a Protein complex structure of sequences from Thermus aquaticus. Full crystallographic information is available from OCA.

Reference

Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase., Campbell EA, Pavlova O, Zenkin N, Leon F, Irschik H, Jansen R, Severinov K, Darst SA, EMBO J. 2005 Feb 23;24(4):674-82. Epub 2005 Feb 3. PMID:15692574

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

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