1cr0: Difference between revisions

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[[Image:1cr0.gif|left|200px]]
[[Image:1cr0.gif|left|200px]]


{{Structure
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{{STRUCTURE_1cr0|  PDB=1cr0 |  SCENE= }}  
|RELATEDENTRY=[[1cr1|1CR1]], [[1cr2|1CR2]], [[1cr4|1CR4]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cr0 OCA], [http://www.ebi.ac.uk/pdbsum/1cr0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cr0 RCSB]</span>
}}


'''CRYSTAL STRUCTURE OF THE HELICASE DOMAIN OF THE GENE4 PROTEIN OF BACTERIOPHAGE T7'''
'''CRYSTAL STRUCTURE OF THE HELICASE DOMAIN OF THE GENE4 PROTEIN OF BACTERIOPHAGE T7'''
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[[Category: Sawaya, M R.]]
[[Category: Sawaya, M R.]]
[[Category: Tabor, S.]]
[[Category: Tabor, S.]]
[[Category: reca-type protein fold]]
[[Category: Reca-type protein fold]]
[[Category: transferase]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:01:33 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:26:53 2008''

Revision as of 13:01, 2 May 2008

File:1cr0.gif

Template:STRUCTURE 1cr0

CRYSTAL STRUCTURE OF THE HELICASE DOMAIN OF THE GENE4 PROTEIN OF BACTERIOPHAGE T7


OverviewOverview

Helicases that unwind DNA at the replication fork are ring-shaped oligomeric enzymes that move along one strand of a DNA duplex and catalyze the displacement of the complementary strand in a reaction that is coupled to nucleotide hydrolysis. The helicase domain of the replicative helicase-primase protein from bacteriophage T7 crystallized as a helical filament that resembles the Escherichia coli RecA protein, an ATP-dependent DNA strand exchange factor. When viewed in projection along the helical axis of the crystals, six protomers of the T7 helicase domain resemble the hexameric rings seen in electron microscopic images of the intact T7 helicase-primase. Nucleotides bind at the interface between pairs of adjacent subunits where an arginine is near the gamma-phosphate of the nucleotide in trans. The bound nucleotide stabilizes the folded conformation of a DNA-binding motif located near the center of the ring. These and other observations suggest how conformational changes are coupled to DNA unwinding activity.

About this StructureAbout this Structure

1CR0 is a Single protein structure of sequence from Enterobacteria phage t7. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7., Sawaya MR, Guo S, Tabor S, Richardson CC, Ellenberger T, Cell. 1999 Oct 15;99(2):167-77. PMID:10535735 Page seeded by OCA on Fri May 2 13:01:33 2008

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