1s67

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[[Image:1s67.jpg|left|200px]]
[[Image:1s67.jpg|left|200px]]
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{{Structure
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|PDB= 1s67 |SIZE=350|CAPTION= <scene name='initialview01'>1s67</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1s67", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>
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|GENE= YDDU, B1489 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1s67| PDB=1s67 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s67 OCA], [http://www.ebi.ac.uk/pdbsum/1s67 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s67 RCSB]</span>
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'''Crystal structure of heme domain of direct oxygen sensor from E. coli'''
'''Crystal structure of heme domain of direct oxygen sensor from E. coli'''
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[[Category: Satterlee, J D.]]
[[Category: Satterlee, J D.]]
[[Category: Suquet, C.]]
[[Category: Suquet, C.]]
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[[Category: e coli]]
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[[Category: E coli]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: oxygen storage/transport]]
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[[Category: Oxygen storage/transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:21:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:37:57 2008''
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Revision as of 05:21, 3 May 2008

Template:STRUCTURE 1s67

Crystal structure of heme domain of direct oxygen sensor from E. coli


Overview

The X-ray crystal structure of the Escherichia coli (Ec) direct oxygen sensor heme domain (Ec DosH) has been solved to 1.8 A using Fe multiple-wavelength anomalous dispersion (MAD), and the positions of Met95 have been confirmed by selenomethionine ((Se)Met) MAD. Ec DosH is the sensing part of a larger two-domain sensing/signaling protein, in which the signaling domain has phosphodiesterase activity. The asymmetric unit of the crystal lattice contains a dimer comprised of two differently ligated heme domain monomers. Except for the heme ligands, the monomer heme domains are identical. In one monomer, the heme is ligated by molecular oxygen (O(2)), while in the other monomer, an endogenous Met95 with S --> Fe ligation replaces the exogenous O(2) ligand. In both heme domains, the proximal ligand is His77. Analysis of these structures reveals sizable ligand-dependent conformational changes in the protein chain localized in the FG turn, the G(beta)-strand, and the HI turn. These changes provide insight to the mechanism of signal propagation within the heme domain following initiation due to O(2) dissociation.

About this Structure

1S67 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)., Park H, Suquet C, Satterlee JD, Kang C, Biochemistry. 2004 Mar 16;43(10):2738-46. PMID:15005609 Page seeded by OCA on Sat May 3 08:21:11 2008

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