1o7l
From Proteopedia
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==Overview== | ==Overview== | ||
| - | ModE is a bacterial transcriptional regulator that orchestrates many, aspects of molybdenum metabolism by binding to specific DNA sequences in a, molybdate-dependent fashion. We present the crystal structure of, Escherichia coli ModE in complex with molybdate, which was determined at, 2.75A from a merohedrally twinned crystal (twin fraction approximately, 0.30) with space group P4(3). We now have structures of ModE in both its, "switched on" (ligand-bound) and "switched off" (apo) states. Comparison, with the apo structure shows that ligand binding leads to extensive, conformational changes not only in the molybdate-binding domain, but also, in the DNA-binding domain. The most obvious difference is the loss of the, pronounced asymmetry between the two chains of the ModE dimer, which had, ... | + | ModE is a bacterial transcriptional regulator that orchestrates many, aspects of molybdenum metabolism by binding to specific DNA sequences in a, molybdate-dependent fashion. We present the crystal structure of, Escherichia coli ModE in complex with molybdate, which was determined at, 2.75A from a merohedrally twinned crystal (twin fraction approximately, 0.30) with space group P4(3). We now have structures of ModE in both its, "switched on" (ligand-bound) and "switched off" (apo) states. Comparison, with the apo structure shows that ligand binding leads to extensive, conformational changes not only in the molybdate-binding domain, but also, in the DNA-binding domain. The most obvious difference is the loss of the, pronounced asymmetry between the two chains of the ModE dimer, which had, been a characteristic property of the apo structure. Another major change, concerns the relative orientation of the two DNA-interacting winged, helix-turn-helix motifs. Manual docking of an idealized DNA structure, suggests that this conformational change should improve DNA binding of the, activated molybdate-bound ModE. |
==About this Structure== | ==About this Structure== | ||
| - | 1O7L is a | + | 1O7L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL, CA and MOO as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: MO1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: winged helix-turn-helix]] | [[Category: winged helix-turn-helix]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:12:38 2007'' |
Revision as of 13:07, 5 November 2007
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MOLYBDATE-ACTIVATED FORM OF MODE FROM ESCHERICHIA COLI
Overview
ModE is a bacterial transcriptional regulator that orchestrates many, aspects of molybdenum metabolism by binding to specific DNA sequences in a, molybdate-dependent fashion. We present the crystal structure of, Escherichia coli ModE in complex with molybdate, which was determined at, 2.75A from a merohedrally twinned crystal (twin fraction approximately, 0.30) with space group P4(3). We now have structures of ModE in both its, "switched on" (ligand-bound) and "switched off" (apo) states. Comparison, with the apo structure shows that ligand binding leads to extensive, conformational changes not only in the molybdate-binding domain, but also, in the DNA-binding domain. The most obvious difference is the loss of the, pronounced asymmetry between the two chains of the ModE dimer, which had, been a characteristic property of the apo structure. Another major change, concerns the relative orientation of the two DNA-interacting winged, helix-turn-helix motifs. Manual docking of an idealized DNA structure, suggests that this conformational change should improve DNA binding of the, activated molybdate-bound ModE.
About this Structure
1O7L is a Single protein structure of sequence from Escherichia coli with CL, CA and MOO as ligands. Structure known Active Site: MO1. Full crystallographic information is available from OCA.
Reference
Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains., Schuttelkopf AW, Boxer DH, Hunter WN, J Mol Biol. 2003 Feb 21;326(3):761-7. PMID:12581638
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