Sandbox Reserved 1687: Difference between revisions
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== <scene name='Ebola_RDRP_Model.pdb'>Ebola Virus RNA-Dependent RNA Polymerase</scene> == | == <scene name='Ebola_RDRP_Model.pdb'>Ebola Virus RNA-Dependent RNA Polymerase</scene> == | ||
<StructureSection load='Ebola_RDRP_Model.pdb' size=' | <StructureSection load='Ebola_RDRP_Model.pdb' size='320' side='right' caption='Ebola Virus RNA-Dependent RNA Polymerase' scene=''> | ||
==Disease== | ==Disease== | ||
A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4. | A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4. | ||
