1o7l
From Proteopedia
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==Overview== | ==Overview== | ||
| - | ModE is a bacterial transcriptional regulator that orchestrates many | + | 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== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hunter, W | + | [[Category: Hunter, W N.]] |
| - | [[Category: Schuttelkopf, A | + | [[Category: Schuttelkopf, A W.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: winged helix-turn-helix]] | [[Category: winged helix-turn-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:20 2008'' |
Revision as of 12:14, 21 February 2008
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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 , and as ligands. Known structural/functional Site: . 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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