1oyy

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[[Image:1oyy.jpg|left|200px]]
[[Image:1oyy.jpg|left|200px]]
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{{Structure
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|PDB= 1oyy |SIZE=350|CAPTION= <scene name='initialview01'>1oyy</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1oyy", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= recQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1oyy| PDB=1oyy | SCENE= }}
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|RELATEDENTRY=[[1owy|1OWY]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyy OCA], [http://www.ebi.ac.uk/pdbsum/1oyy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oyy RCSB]</span>
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}}
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'''Structure of the RecQ Catalytic Core bound to ATP-gamma-S'''
'''Structure of the RecQ Catalytic Core bound to ATP-gamma-S'''
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[[Category: Keck, J L.]]
[[Category: Keck, J L.]]
[[Category: Zittel, M C.]]
[[Category: Zittel, M C.]]
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[[Category: atp binding]]
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[[Category: Atp binding]]
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[[Category: atp(gamma)]]
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[[Category: Helicase]]
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[[Category: helicase]]
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[[Category: Helix-turn-helix]]
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[[Category: helix-turn-helix]]
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[[Category: Recq]]
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[[Category: recq]]
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[[Category: Winged helix]]
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[[Category: winged helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:27:00 2008''
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[[Category: zn(2+) binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:52:24 2008''
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Revision as of 01:27, 3 May 2008

Template:STRUCTURE 1oyy

Structure of the RecQ Catalytic Core bound to ATP-gamma-S


Overview

RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to the ATP analog ATPgammaS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn(2+)-binding and winged-helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ-associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.

About this Structure

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

Reference

High-resolution structure of the E.coli RecQ helicase catalytic core., Bernstein DA, Zittel MC, Keck JL, EMBO J. 2003 Oct 1;22(19):4910-21. PMID:14517231 Page seeded by OCA on Sat May 3 04:27:00 2008

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