1bdj: Difference between revisions
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==Overview== | ==Overview== | ||
The three-dimensional structure of the HPt domain of ArcB complexed with, CheY has been determined using the molecular-replacement method. The, structure was refined to a crystallographic R factor of 18.3% at 2.68 A, resolution. The final model included 1899 protein atoms (117 residues from, the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent, molecules. In the crystal, CheY molecules stacked along the a axis of the, cell with no interactions between neighbouring rows and the HPt domain, bridged the CheY molecules. The phosphodonor residue His715 was fully, exposed to the solvent region, even though the HPt domain was in contact, with four molecules of CheY. CheY showed significant conformational, change. This indicates that the HPt domain has a rigid structure . | The three-dimensional structure of the HPt domain of ArcB complexed with, CheY has been determined using the molecular-replacement method. The, structure was refined to a crystallographic R factor of 18.3% at 2.68 A, resolution. The final model included 1899 protein atoms (117 residues from, the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent, molecules. In the crystal, CheY molecules stacked along the a axis of the, cell with no interactions between neighbouring rows and the HPt domain, bridged the CheY molecules. The phosphodonor residue His715 was fully, exposed to the solvent region, even though the HPt domain was in contact, with four molecules of CheY. CheY showed significant conformational, change. This indicates that the HPt domain has a rigid structure when, complexed with CheY. | ||
==About this Structure== | ==About this Structure== | ||
1BDJ is a | 1BDJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: PHA and PHD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BDJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: two-component system]] | [[Category: two-component system]] | ||
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Revision as of 14:12, 5 November 2007
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COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY
OverviewOverview
The three-dimensional structure of the HPt domain of ArcB complexed with, CheY has been determined using the molecular-replacement method. The, structure was refined to a crystallographic R factor of 18.3% at 2.68 A, resolution. The final model included 1899 protein atoms (117 residues from, the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent, molecules. In the crystal, CheY molecules stacked along the a axis of the, cell with no interactions between neighbouring rows and the HPt domain, bridged the CheY molecules. The phosphodonor residue His715 was fully, exposed to the solvent region, even though the HPt domain was in contact, with four molecules of CheY. CheY showed significant conformational, change. This indicates that the HPt domain has a rigid structure when, complexed with CheY.
About this StructureAbout this Structure
1BDJ is a Protein complex structure of sequences from Escherichia coli with SO4 as ligand. Structure known Active Sites: PHA and PHD. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY., Kato M, Shimizu T, Mizuno T, Hakoshima T, Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1257-63. PMID:10393292
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