1eyv: Difference between revisions

Revision as of 13:33, 21 February 2008

THE CRYSTAL STRUCTURE OF NUSB FROM MYCOBACTERIUM TUBERCULOSIS

OverviewOverview

Both prokaryotes and eukaryotes regulate transcription through mechanisms that suppress termination signals. An antitermination mechanism was first characterized in bacteriophage lambda. Bacteria have analogous machinery that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage lambda N protein) substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal structure of NusB from Mycobacterium tuberculosis, the bacterium that causes tuberculosis in humans. This molecule shares a similar tertiary structure with the related Escherichia coli protein but adopts a different quaternary organization. We show that, unlike the E. coli homolog, M. tuberculosis NusB is dimeric both in solution and in the crystal. These data help provide a framework for understanding the structural and biological function of NusB in the prokaryotic transcriptional antitermination complex.

About this StructureAbout this Structure

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

ReferenceReference

The crystal structure of NusB from Mycobacterium tuberculosis., Gopal B, Haire LF, Cox RA, Jo Colston M, Major S, Brannigan JA, Smerdon SJ, Dodson G, Nat Struct Biol. 2000 Jun;7(6):475-8. PMID:10881194

Page seeded by OCA on Thu Feb 21 12:32:59 2008

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OCA

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-[[Image:1eyv.gif|left|200px]]<br /><applet load="1eyv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1eyv.gif|left|200px]]<br /><applet load="1eyv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1eyv, resolution 1.6&Aring;" />
 '''THE CRYSTAL STRUCTURE OF NUSB FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
 ==Overview==
-Both prokaryotes and eukaryotes regulate transcription through mechanisms, that suppress termination signals. An antitermination mechanism was first, characterized in bacteriophage lambda. Bacteria have analogous machinery, that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage lambda N protein), substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal, structure of NusB from Mycobacterium tuberculosis, the bacterium that, causes tuberculosis in humans. This molecule shares a similar tertiary, structure with the related Escherichia coli protein but adopts a different, quaternary organization. We show that, unlike the E. coli homolog, M., tuberculosis NusB is dimeric both in solution and in the crystal. These, data help provide a framework for understanding the structural and, biological function of NusB in the prokaryotic transcriptional, antitermination complex.
+Both prokaryotes and eukaryotes regulate transcription through mechanisms that suppress termination signals. An antitermination mechanism was first characterized in bacteriophage lambda. Bacteria have analogous machinery that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage lambda N protein) substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal structure of NusB from Mycobacterium tuberculosis, the bacterium that causes tuberculosis in humans. This molecule shares a similar tertiary structure with the related Escherichia coli protein but adopts a different quaternary organization. We show that, unlike the E. coli homolog, M. tuberculosis NusB is dimeric both in solution and in the crystal. These data help provide a framework for understanding the structural and biological function of NusB in the prokaryotic transcriptional antitermination complex.
 ==About this Structure==
-EYV 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EYV OCA].
+EYV 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYV OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mycobacterium tuberculosis]]
 [[Category: Single protein]]
-[[Category: Brannigan, J.A.]]
+[[Category: Brannigan, J A.]]
-[[Category: Colston, M.J.]]
+[[Category: Colston, M J.]]
-[[Category: Cox, R.A.]]
+[[Category: Cox, R A.]]
-[[Category: Dodson, G.G.]]
+[[Category: Dodson, G G.]]
 [[Category: Gopal, B.]]
-[[Category: Haire, L.F.]]
+[[Category: Haire, L F.]]
 [[Category: Major, S.]]
-[[Category: Smerdon, S.J.]]
+[[Category: Smerdon, S J.]]
-[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
+[[Category: TBSGC, TB Structural Genomics Consortium.]]
 [[Category: PO4]]
 [[Category: helical bundle]]
@@ Line 30: / Line 30: @@
 [[Category: tbsgc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:26:45 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:59 2008''