1uaa

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(New page: 200px<br /><applet load="1uaa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uaa, resolution 3.000&Aring;" /> '''E. COLI REP HELICAS...)
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caption="1uaa, resolution 3.000&Aring;" />
'''E. COLI REP HELICASE/DNA COMPLEX'''<br />
'''E. COLI REP HELICASE/DNA COMPLEX'''<br />
==Overview==
==Overview==
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Crystal structures of binary and ternary complexes of the E. coli Rep, helicase bound to single-stranded (ss) DNA or ssDNA and ADP were, determined to a resolution of 3.0 A and 3.2 A, respectively. The, asymmetric unit in the crystals contains two Rep monomers differing from, each other by a large reorientation of one of the domains, corresponding, to a swiveling of 130 degrees about a hinge region. Such domain movements, are sufficiently large to suggest that these may be coupled to, translocation of the Rep dimer along DNA. The ssDNA binding site involves, the helicase motifs Ia, III, and V, whereas the ADP binding site involves, helicase motifs I and IV. Residues in motifs II and VI may function to, transduce the allosteric effects of nucleotides on DNA binding. These, structures represent the first view of a DNA helicase bound to DNA.
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Crystal structures of binary and ternary complexes of the E. coli Rep helicase bound to single-stranded (ss) DNA or ssDNA and ADP were determined to a resolution of 3.0 A and 3.2 A, respectively. The asymmetric unit in the crystals contains two Rep monomers differing from each other by a large reorientation of one of the domains, corresponding to a swiveling of 130 degrees about a hinge region. Such domain movements are sufficiently large to suggest that these may be coupled to translocation of the Rep dimer along DNA. The ssDNA binding site involves the helicase motifs Ia, III, and V, whereas the ADP binding site involves helicase motifs I and IV. Residues in motifs II and VI may function to transduce the allosteric effects of nucleotides on DNA binding. These structures represent the first view of a DNA helicase bound to DNA.
==About this Structure==
==About this Structure==
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1UAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UAA OCA].
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1UAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAA OCA].
==Reference==
==Reference==
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[[Category: helicase]]
[[Category: helicase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:17 2008''

Revision as of 13:22, 21 February 2008


1uaa, resolution 3.000Å

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E. COLI REP HELICASE/DNA COMPLEX

Overview

Crystal structures of binary and ternary complexes of the E. coli Rep helicase bound to single-stranded (ss) DNA or ssDNA and ADP were determined to a resolution of 3.0 A and 3.2 A, respectively. The asymmetric unit in the crystals contains two Rep monomers differing from each other by a large reorientation of one of the domains, corresponding to a swiveling of 130 degrees about a hinge region. Such domain movements are sufficiently large to suggest that these may be coupled to translocation of the Rep dimer along DNA. The ssDNA binding site involves the helicase motifs Ia, III, and V, whereas the ADP binding site involves helicase motifs I and IV. Residues in motifs II and VI may function to transduce the allosteric effects of nucleotides on DNA binding. These structures represent the first view of a DNA helicase bound to DNA.

About this Structure

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

Reference

Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP., Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G, Cell. 1997 Aug 22;90(4):635-47. PMID:9288744

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