2b2n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2b2n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b2n, resolution 2.10&Aring;" /> '''Structure of transcr...)
Line 1: Line 1:
-
[[Image:2b2n.gif|left|200px]]<br /><applet load="2b2n" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2b2n.gif|left|200px]]<br /><applet load="2b2n" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2b2n, resolution 2.10&Aring;" />
caption="2b2n, resolution 2.10&Aring;" />
'''Structure of transcription-repair coupling factor'''<br />
'''Structure of transcription-repair coupling factor'''<br />
==Overview==
==Overview==
-
The transcription repair coupling factor Mfd removes stalled RNA, polymerase from DNA lesions and links transcription to UvrABC-dependent, nucleotide excision repair in prokaryotes. We report the 2.1A crystal, structure of the UvrA-binding N terminus (residues 1-333) of Escherichia, coli Mfd (Mfd-N). Remarkably, Mfd-N reveals a fold that resembles the, three N-terminal domains of the repair enzyme UvrB. Domain 1A of Mfd, adopts a typical RecA fold, domain 1B matches the damage-binding domain of, the UvrB, and domain 2 highly resembles the implicated UvrA-binding domain, of UvrB. However, Mfd apparently lacks a functional ATP-binding site and, does not contain the DNA damage-binding motifs of UvrB. Thus, our results, suggest that Mfd might form a UvrA recruitment factor at stalled, transcription complexes that architecturally but not catalytically, resembles UvrB.
+
The transcription repair coupling factor Mfd removes stalled RNA polymerase from DNA lesions and links transcription to UvrABC-dependent nucleotide excision repair in prokaryotes. We report the 2.1A crystal structure of the UvrA-binding N terminus (residues 1-333) of Escherichia coli Mfd (Mfd-N). Remarkably, Mfd-N reveals a fold that resembles the three N-terminal domains of the repair enzyme UvrB. Domain 1A of Mfd adopts a typical RecA fold, domain 1B matches the damage-binding domain of the UvrB, and domain 2 highly resembles the implicated UvrA-binding domain of UvrB. However, Mfd apparently lacks a functional ATP-binding site and does not contain the DNA damage-binding motifs of UvrB. Thus, our results suggest that Mfd might form a UvrA recruitment factor at stalled transcription complexes that architecturally but not catalytically resembles UvrB.
==About this Structure==
==About this Structure==
-
2B2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NA, SO4 and P4C as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B2N OCA].
+
2B2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=P4C:'>P4C</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B2N OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Assenmacher, N.]]
[[Category: Assenmacher, N.]]
-
[[Category: Hopfner, K.P.]]
+
[[Category: Hopfner, K P.]]
[[Category: Lammens, A.]]
[[Category: Lammens, A.]]
[[Category: Wenig, K.]]
[[Category: Wenig, K.]]
Line 22: Line 22:
[[Category: x-ray crystallography; strand-specific repair; template strand; rna polymerase; rnap; uvra/b/c repair system]]
[[Category: x-ray crystallography; strand-specific repair; template strand; rna polymerase; rnap; uvra/b/c repair system]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:32:13 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:15 2008''

Revision as of 14:34, 21 February 2008


2b2n, resolution 2.10Å

Drag the structure with the mouse to rotate

Structure of transcription-repair coupling factor

Overview

The transcription repair coupling factor Mfd removes stalled RNA polymerase from DNA lesions and links transcription to UvrABC-dependent nucleotide excision repair in prokaryotes. We report the 2.1A crystal structure of the UvrA-binding N terminus (residues 1-333) of Escherichia coli Mfd (Mfd-N). Remarkably, Mfd-N reveals a fold that resembles the three N-terminal domains of the repair enzyme UvrB. Domain 1A of Mfd adopts a typical RecA fold, domain 1B matches the damage-binding domain of the UvrB, and domain 2 highly resembles the implicated UvrA-binding domain of UvrB. However, Mfd apparently lacks a functional ATP-binding site and does not contain the DNA damage-binding motifs of UvrB. Thus, our results suggest that Mfd might form a UvrA recruitment factor at stalled transcription complexes that architecturally but not catalytically resembles UvrB.

About this Structure

2B2N is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for transcription-coupled repair: the N terminus of Mfd resembles UvrB with degenerate ATPase motifs., Assenmacher N, Wenig K, Lammens A, Hopfner KP, J Mol Biol. 2006 Jan 27;355(4):675-83. Epub 2005 Nov 8. PMID:16309703

Page seeded by OCA on Thu Feb 21 16:34:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools