1h9s: Difference between revisions

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[[Image:1h9s.jpg|left|200px]]
{{Seed}}
[[Image:1h9s.png|left|200px]]


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{{STRUCTURE_1h9s|  PDB=1h9s  |  SCENE=  }}  
{{STRUCTURE_1h9s|  PDB=1h9s  |  SCENE=  }}  


'''MOLYBDATE BOUND COMPLEX OF DIMOP DOMAIN OF MODE FROM E.COLI'''
===MOLYBDATE BOUND COMPLEX OF DIMOP DOMAIN OF MODE FROM E.COLI===




==Overview==
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The molybdate-dependent transcriptional regulator ModE of Escherichia coli functions as a sensor of intracellular molybdate concentration and a regulator for the transcription of several operons that control the uptake and utilization of molybdenum. We present two high-resolution crystal structures of the C-terminal oxyanion-binding domain in complex with molybdate and tungstate. The ligands bind between subunits at the dimerization interface, and analysis reveals that oxyanion selectivity is determined primarily by size. The relevance of the structures is indicated by fluorescence measurements, which show that the oxyanion binding properties of the C-terminal domain of ModE are similar to those of the full-length protein. Comparisons with the apoprotein structure have identified structural rearrangements that occur on binding oxyanion. This molybdate-dependent conformational switch promotes a change in shape and alterations to the surface of the protein and may provide the signal for recruitment of other proteins to construct the machinery for transcription. Sequence and structure-based comparisons lead to a classification of molybdate-binding proteins.
The line below this paragraph, {{ABSTRACT_PUBMED_11259434}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11259434}}


==About this Structure==
==About this Structure==
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[[Category: Hunter, W N.]]
[[Category: Hunter, W N.]]
[[Category: Transcription regulator]]
[[Category: Transcription regulator]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:36:54 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:51:55 2008''

Revision as of 04:51, 1 July 2008

File:1h9s.png

Template:STRUCTURE 1h9s

MOLYBDATE BOUND COMPLEX OF DIMOP DOMAIN OF MODE FROM E.COLI

Template:ABSTRACT PUBMED 11259434

About this Structure

1H9S is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Oxyanion binding alters conformation and quaternary structure of the c-terminal domain of the transcriptional regulator mode. Implications for molybdate-dependent regulation, signaling, storage, and transport., Gourley DG, Schuttelkopf AW, Anderson LA, Price NC, Boxer DH, Hunter WN, J Biol Chem. 2001 Jun 8;276(23):20641-7. Epub 2001 Mar 20. PMID:11259434

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