1u5k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1u5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u5k, resolution 2.00&Aring;" /> '''Recombinational repa...)
Line 1: Line 1:
-
[[Image:1u5k.jpg|left|200px]]<br /><applet load="1u5k" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1u5k.jpg|left|200px]]<br /><applet load="1u5k" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u5k, resolution 2.00&Aring;" />
caption="1u5k, resolution 2.00&Aring;" />
'''Recombinational repair protein RecO'''<br />
'''Recombinational repair protein RecO'''<br />
==Overview==
==Overview==
-
Recovery of arrested replication requires coordinated action of DNA, repair, replication, and recombination machineries. Bacterial RecO protein, is a member of RecF recombination repair pathway important for replication, recovery. RecO possesses two distinct activities in vitro, closely, resembling those of eukaryotic protein Rad52: DNA annealing and, RecA-mediated DNA recombination. Here we present the crystal structure of, the RecO protein from the extremely radiation resistant bacteria, Deinococcus radiodurans (DrRecO) and characterize its DNA binding and, strand annealing properties. The RecO structure is totally different from, the Rad52 structure. DrRecO is comprised of three structural domains: an, N-terminal domain which adopts an OB-fold, a novel alpha-helical domain, and an unusual zinc-binding domain. Sequence alignments suggest that the, multidomain architecture is conserved between RecO proteins from other, bacterial species and is suitable to elucidate sites of protein-protein, and DNA-protein interactions necessary for RecO functions during the, replication recovery and DNA repair.
+
Recovery of arrested replication requires coordinated action of DNA repair, replication, and recombination machineries. Bacterial RecO protein is a member of RecF recombination repair pathway important for replication recovery. RecO possesses two distinct activities in vitro, closely resembling those of eukaryotic protein Rad52: DNA annealing and RecA-mediated DNA recombination. Here we present the crystal structure of the RecO protein from the extremely radiation resistant bacteria Deinococcus radiodurans (DrRecO) and characterize its DNA binding and strand annealing properties. The RecO structure is totally different from the Rad52 structure. DrRecO is comprised of three structural domains: an N-terminal domain which adopts an OB-fold, a novel alpha-helical domain, and an unusual zinc-binding domain. Sequence alignments suggest that the multidomain architecture is conserved between RecO proteins from other bacterial species and is suitable to elucidate sites of protein-protein and DNA-protein interactions necessary for RecO functions during the replication recovery and DNA repair.
==About this Structure==
==About this Structure==
-
1U5K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans_r1 Deinococcus radiodurans r1] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U5K OCA].
+
1U5K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans_r1 Deinococcus radiodurans r1] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5K OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bera, S.]]
[[Category: Bera, S.]]
-
[[Category: Grandgenett, D.P.]]
+
[[Category: Grandgenett, D P.]]
[[Category: Korolev, S.]]
[[Category: Korolev, S.]]
[[Category: Koroleva, O.]]
[[Category: Koroleva, O.]]
Line 22: Line 22:
[[Category: zn-binding]]
[[Category: zn-binding]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:21:02 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:52 2008''

Revision as of 13:20, 21 February 2008


1u5k, resolution 2.00Å

Drag the structure with the mouse to rotate

Recombinational repair protein RecO

Overview

Recovery of arrested replication requires coordinated action of DNA repair, replication, and recombination machineries. Bacterial RecO protein is a member of RecF recombination repair pathway important for replication recovery. RecO possesses two distinct activities in vitro, closely resembling those of eukaryotic protein Rad52: DNA annealing and RecA-mediated DNA recombination. Here we present the crystal structure of the RecO protein from the extremely radiation resistant bacteria Deinococcus radiodurans (DrRecO) and characterize its DNA binding and strand annealing properties. The RecO structure is totally different from the Rad52 structure. DrRecO is comprised of three structural domains: an N-terminal domain which adopts an OB-fold, a novel alpha-helical domain, and an unusual zinc-binding domain. Sequence alignments suggest that the multidomain architecture is conserved between RecO proteins from other bacterial species and is suitable to elucidate sites of protein-protein and DNA-protein interactions necessary for RecO functions during the replication recovery and DNA repair.

About this Structure

1U5K is a Single protein structure of sequence from Deinococcus radiodurans r1 with as ligand. Full crystallographic information is available from OCA.

Reference

A novel structure of DNA repair protein RecO from Deinococcus radiodurans., Makharashvili N, Koroleva O, Bera S, Grandgenett DP, Korolev S, Structure. 2004 Oct;12(10):1881-9. PMID:15458636

Page seeded by OCA on Thu Feb 21 15:20:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools