1ey1

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(New page: 200px<br /><applet load="1ey1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ey1" /> '''SOLUTION STRUCTURE OF ESCHERICHIA COLI NUSB'...)
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[[Image:1ey1.jpg|left|200px]]<br /><applet load="1ey1" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF ESCHERICHIA COLI NUSB'''<br />
'''SOLUTION STRUCTURE OF ESCHERICHIA COLI NUSB'''<br />
==Overview==
==Overview==
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We have determined the solution structure of NusB, a transcription, antitermination protein from Escherichia coli. The structure reveals a, novel, all alpha-helical protein fold. NusB mutations that cause a loss of, function (NusB5) or alter specificity for RNA targets (NusB101) are, localized to surface residues and likely affect RNA-protein or, protein-protein interactions. Residues that are highly conserved among, homologs stabilize the protein core. The solution structure of E. coli, NusB presented here resembles that of Mycobacterium tuberculosis NusB, determined by X-ray diffraction, but differs substantially from a solution, structure of E. coli NusB reported earlier.
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We have determined the solution structure of NusB, a transcription antitermination protein from Escherichia coli. The structure reveals a novel, all alpha-helical protein fold. NusB mutations that cause a loss of function (NusB5) or alter specificity for RNA targets (NusB101) are localized to surface residues and likely affect RNA-protein or protein-protein interactions. Residues that are highly conserved among homologs stabilize the protein core. The solution structure of E. coli NusB presented here resembles that of Mycobacterium tuberculosis NusB determined by X-ray diffraction, but differs substantially from a solution structure of E. coli NusB reported earlier.
==About this Structure==
==About this Structure==
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1EY1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EY1 OCA].
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1EY1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY1 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Altieri, A.S.]]
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[[Category: Altieri, A S.]]
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[[Category: Coats, R.H.]]
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[[Category: Coats, R H.]]
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[[Category: Horita, D.A.]]
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[[Category: Horita, D A.]]
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[[Category: Mazzulla, M.J.]]
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[[Category: Mazzulla, M J.]]
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[[Category: Wingfield, P.T.]]
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[[Category: Wingfield, P T.]]
[[Category: transcirption termination]]
[[Category: transcirption termination]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:24:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:42 2008''

Revision as of 10:32, 21 February 2008


1ey1

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SOLUTION STRUCTURE OF ESCHERICHIA COLI NUSB

Overview

We have determined the solution structure of NusB, a transcription antitermination protein from Escherichia coli. The structure reveals a novel, all alpha-helical protein fold. NusB mutations that cause a loss of function (NusB5) or alter specificity for RNA targets (NusB101) are localized to surface residues and likely affect RNA-protein or protein-protein interactions. Residues that are highly conserved among homologs stabilize the protein core. The solution structure of E. coli NusB presented here resembles that of Mycobacterium tuberculosis NusB determined by X-ray diffraction, but differs substantially from a solution structure of E. coli NusB reported earlier.

About this Structure

1EY1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structure of the transcriptional antiterminator NusB from Escherichia coli., Altieri AS, Mazzulla MJ, Horita DA, Coats RH, Wingfield PT, Das A, Court DL, Byrd RA, Nat Struct Biol. 2000 Jun;7(6):470-4. PMID:10881193

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