2b2n: Difference between revisions
New page: left|200px<br /><applet load="2b2n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b2n, resolution 2.10Å" /> '''Structure of transcr... |
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[[Image:2b2n.gif|left|200px]]<br /><applet load="2b2n" size=" | [[Image:2b2n.gif|left|200px]]<br /><applet load="2b2n" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2b2n, resolution 2.10Å" /> | caption="2b2n, resolution 2.10Å" /> | ||
'''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 | 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:// | 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Assenmacher, N.]] | [[Category: Assenmacher, N.]] | ||
[[Category: Hopfner, K | [[Category: Hopfner, K P.]] | ||
[[Category: Lammens, A.]] | [[Category: Lammens, A.]] | ||
[[Category: Wenig, K.]] | [[Category: Wenig, K.]] | ||
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[[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:// | ''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
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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 NA, SO4 and P4C 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
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