1o7l: Difference between revisions
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[[Image:1o7l.jpg|left|200px]] | [[Image:1o7l.jpg|left|200px]] | ||
'''MOLYBDATE-ACTIVATED FORM OF MODE FROM ESCHERICHIA COLI''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MOO:MOLYBDATE ION'>MOO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''MOLYBDATE-ACTIVATED FORM OF MODE FROM ESCHERICHIA COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1O7L is a [ | 1O7L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7L OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12581638 12581638] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:50 2008'' | ||
Revision as of 11:06, 20 March 2008
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| 1o7l, resolution 2.75Å | |||||||||||||
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| Sites: | MO1 | ||||||||||||
| Ligands: | CL, CA and MOO | ||||||||||||
| 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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