1uaa
From Proteopedia
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| - | [[Image:1uaa.jpg|left|200px]] | + | [[Image:1uaa.jpg|left|200px]] |
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| - | '''E. COLI REP HELICASE/DNA COMPLEX''' | + | {{Structure |
| + | |PDB= 1uaa |SIZE=350|CAPTION= <scene name='initialview01'>1uaa</scene>, resolution 3.000Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''E. COLI REP HELICASE/DNA COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UAA is a [ | + | 1UAA is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9288744 9288744] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helicase]] | [[Category: helicase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:29:23 2008'' |
Revision as of 12:29, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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