1k0r

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(New page: 200px<br /><applet load="1k0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k0r, resolution 1.70&Aring;" /> '''Crystal Structure of...)
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'''Crystal Structure of Mycobacterium tuberculosis NusA'''<br />
'''Crystal Structure of Mycobacterium tuberculosis NusA'''<br />
==Overview==
==Overview==
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Mycobacterium tuberculosis is the cause of tuberculosis in humans, a, disease that affects over a one-third of the world's population. This, slow-growing pathogen has only one ribosomal RNA operon, thus making its, transcriptional apparatus a fundamentally interesting target for drug, discovery. NusA binds to RNA polymerase and modulates several of the, ribosomal RNA transcriptional processes. Here, we report the crystal, structure of NusA, and reveal that the molecule consists of four domains., They are organised as two distinct entities. The N-terminal domain, (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding, cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329), consisting of a ribosomal S1 protein domain followed by two K homology, domains. The S1 and KH domains are tightly integrated together to form an, extensive RNA-binding structure, but are flexibly tethered to the, N-terminal domain. The molecule's surfaces and architecture provide, insights into RNA and polymerase interactions and the mechanism of pause, site discrimination. They also allow us to rationalize certain, termination-defective and cold shock-sensitive mutations in the nusA gene, that have been studied in Escherichia coli.
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Mycobacterium tuberculosis is the cause of tuberculosis in humans, a disease that affects over a one-third of the world's population. This slow-growing pathogen has only one ribosomal RNA operon, thus making its transcriptional apparatus a fundamentally interesting target for drug discovery. NusA binds to RNA polymerase and modulates several of the ribosomal RNA transcriptional processes. Here, we report the crystal structure of NusA, and reveal that the molecule consists of four domains. They are organised as two distinct entities. The N-terminal domain (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329) consisting of a ribosomal S1 protein domain followed by two K homology domains. The S1 and KH domains are tightly integrated together to form an extensive RNA-binding structure, but are flexibly tethered to the N-terminal domain. The molecule's surfaces and architecture provide insights into RNA and polymerase interactions and the mechanism of pause site discrimination. They also allow us to rationalize certain termination-defective and cold shock-sensitive mutations in the nusA gene that have been studied in Escherichia coli.
==About this Structure==
==About this Structure==
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1K0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K0R OCA].
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1K0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0R OCA].
==Reference==
==Reference==
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Colston, M.J.]]
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[[Category: Colston, M J.]]
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[[Category: Dodson, E.J.]]
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[[Category: Dodson, E J.]]
[[Category: Dodson, G.]]
[[Category: Dodson, G.]]
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[[Category: Gamblin, S.J.]]
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[[Category: Gamblin, S J.]]
[[Category: Gopal, B.]]
[[Category: Gopal, B.]]
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[[Category: Haire, L.F.]]
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[[Category: Haire, L F.]]
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[[Category: Lane, A.N.]]
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[[Category: Lane, A N.]]
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[[Category: Papavinasasundaram, K.G.]]
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[[Category: Papavinasasundaram, K G.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
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[[Category: two k-homology domains.]]
[[Category: two k-homology domains.]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:45:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:49 2008''

Revision as of 11:28, 21 February 2008


1k0r, resolution 1.70Å

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Crystal Structure of Mycobacterium tuberculosis NusA

Overview

Mycobacterium tuberculosis is the cause of tuberculosis in humans, a disease that affects over a one-third of the world's population. This slow-growing pathogen has only one ribosomal RNA operon, thus making its transcriptional apparatus a fundamentally interesting target for drug discovery. NusA binds to RNA polymerase and modulates several of the ribosomal RNA transcriptional processes. Here, we report the crystal structure of NusA, and reveal that the molecule consists of four domains. They are organised as two distinct entities. The N-terminal domain (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329) consisting of a ribosomal S1 protein domain followed by two K homology domains. The S1 and KH domains are tightly integrated together to form an extensive RNA-binding structure, but are flexibly tethered to the N-terminal domain. The molecule's surfaces and architecture provide insights into RNA and polymerase interactions and the mechanism of pause site discrimination. They also allow us to rationalize certain termination-defective and cold shock-sensitive mutations in the nusA gene that have been studied in Escherichia coli.

About this Structure

1K0R is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution., Gopal B, Haire LF, Gamblin SJ, Dodson EJ, Lane AN, Papavinasasundaram KG, Colston MJ, Dodson G, J Mol Biol. 2001 Dec 14;314(5):1087-95. PMID:11743725

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