1qhh: Difference between revisions
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[[Image:1qhh.jpg|left|200px]] | [[Image:1qhh.jpg|left|200px]] | ||
'''STRUCTURE OF DNA HELICASE WITH ADPNP''' | {{Structure | ||
|PDB= 1qhh |SIZE=350|CAPTION= <scene name='initialview01'>1qhh</scene>, resolution 2.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |||
|ACTIVITY= | |||
|GENE= PCRA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus]) | |||
}} | |||
'''STRUCTURE OF DNA HELICASE WITH ADPNP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QHH is a [ | 1QHH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHH OCA]. | ||
==Reference== | ==Reference== | ||
DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase., Soultanas P, Dillingham MS, Velankar SS, Wigley DB, J Mol Biol. 1999 Jul 2;290(1):137-48. PMID:[http:// | DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase., Soultanas P, Dillingham MS, Velankar SS, Wigley DB, J Mol Biol. 1999 Jul 2;290(1):137-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10388562 10388562] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: sos response]] | [[Category: sos response]] | ||
''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 13:37:31 2008'' | ||
Revision as of 14:37, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | PCRA (Geobacillus stearothermophilus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF DNA HELICASE WITH ADPNP
OverviewOverview
Based upon the crystal structures of PcrA helicase, we have made and characterised mutations in a number of conserved helicase signature motifs around the ATPase active site. We have also determined structures of complexes of wild-type PcrA with ADPNP and of a mutant PcrA complexed with ADPNP and Mn2+. The kinetic and structural data define roles for a number of different residues in and around the ATP binding site. More importantly, our results also show that there are two functionally distinct conformations of ATP in the active site. In one conformation, ATP is hydrolysed poorly whereas in the other (activated) conformation, ATP is hydrolysed much more rapidly. We propose a mechanism to explain how the stimulation of ATPase activity afforded by binding of single-stranded DNA stabilises the activated conformation favouring Mg2+binding and a consequent repositioning of the gamma-phosphate group which promotes ATP hydrolysis. A part of the associated conformational change in the protein forces the side-chain of K37 to vacate the Mg2+binding site, allowing the cation to bind and interact with ATP.
About this StructureAbout this Structure
1QHH is a Protein complex structure of sequences from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
ReferenceReference
DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase., Soultanas P, Dillingham MS, Velankar SS, Wigley DB, J Mol Biol. 1999 Jul 2;290(1):137-48. PMID:10388562
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