1o7l
From Proteopedia
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|PDB= 1o7l |SIZE=350|CAPTION= <scene name='initialview01'>1o7l</scene>, resolution 2.75Å | |PDB= 1o7l |SIZE=350|CAPTION= <scene name='initialview01'>1o7l</scene>, resolution 2.75Å | ||
|SITE= <scene name='pdbsite=MO1:Ca+Binding+Site+For+Chain+D'>MO1</scene> | |SITE= <scene name='pdbsite=MO1:Ca+Binding+Site+For+Chain+D'>MO1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7l OCA], [http://www.ebi.ac.uk/pdbsum/1o7l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o7l RCSB]</span> | ||
}} | }} | ||
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[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
[[Category: Schuttelkopf, A W.]] | [[Category: Schuttelkopf, A W.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MOO]] | ||
| - | [[Category: activator]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
[[Category: molybdate]] | [[Category: molybdate]] | ||
[[Category: mop]] | [[Category: mop]] | ||
| - | [[Category: transcriptional regulator]] | + | [[Category: transcriptional regulator,activator]] |
[[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 Sun Mar 30 22:41:03 2008'' |
Revision as of 19:41, 30 March 2008
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| , resolution 2.75Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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