1v9y: Difference between revisions

Revision as of 17:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v9y.png

Template:STRUCTURE 1v9y

Crystal Structure of the heme PAS sensor domain of Ec DOS (ferric form)Crystal Structure of the heme PAS sensor domain of Ec DOS (ferric form)

Template:ABSTRACT PUBMED 14982921

About this StructureAbout this Structure

1V9Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor., Kurokawa H, Lee DS, Watanabe M, Sagami I, Mikami B, Raman CS, Shimizu T, J Biol Chem. 2004 May 7;279(19):20186-93. Epub 2004 Feb 23. PMID:14982921

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of the heme PAS sensor domain of Ec DOS (ferric form)'''
+===Crystal Structure of the heme PAS sensor domain of Ec DOS (ferric form)===
-==Overview==
+<!--
-PAS domains, which have been identified in over 1100 proteins from all three kingdoms of life, convert various input stimuli into signals that propagate to downstream components by modifying protein-protein interactions. One such protein is the Escherichia coli redox sensor, Ec DOS, a phosphodiesterase that degrades cyclic adenosine monophosphate in a redox-dependent manner. Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively. The protein folds into a characteristic PAS domain structure and forms a homodimer. In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule. Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other. The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
+The line below this paragraph, {{ABSTRACT_PUBMED_14982921}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14982921 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14982921}}
 ==About this Structure==
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 [[Category: Pa]]
 [[Category: Sensor]]
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