Tom Sandbox

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{{STRUCTURE_1d66| PDB=1d66 | SCENE= }}
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===DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX===
===DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX===
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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, <scene name='Tom_Sandbox/Cd_binding/1'>Zn(2+)-containing domain </scene>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, <scene name='Tom_Sandbox/Cd_binding/1'>Zn(2+)-containing domain </scene>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.
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{{STRUCTURE_1YSA| PDB=1YSA | SCENE= }}
==About this Structure==
==About this Structure==

Revision as of 21:36, 8 November 2011

Image:2ZTA.png


Template:STRUCTURE 2ZTA

Contents

DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX

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, 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.

Template:STRUCTURE 1YSA

About this Structure

1d66 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

See Also

Reference

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Alan Tom

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