1s67
From Proteopedia
(New page: 200px<br /><applet load="1s67" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s67, resolution 1.5Å" /> '''Crystal structure of ...) |
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| - | [[Image:1s67.jpg|left|200px]]<br /><applet load="1s67" size=" | + | [[Image:1s67.jpg|left|200px]]<br /><applet load="1s67" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s67, resolution 1.5Å" /> | caption="1s67, resolution 1.5Å" /> | ||
'''Crystal structure of heme domain of direct oxygen sensor from E. coli'''<br /> | '''Crystal structure of heme domain of direct oxygen sensor from E. coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of the Escherichia coli (Ec) direct oxygen | + | 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== | ==About this Structure== | ||
| - | 1S67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1S67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S67 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kang, C | + | [[Category: Kang, C H.]] |
| - | [[Category: Park, H | + | [[Category: Park, H J.]] |
| - | [[Category: Satterlee, J | + | [[Category: Satterlee, J D.]] |
[[Category: Suquet, C.]] | [[Category: Suquet, C.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: OXY]] | [[Category: OXY]] | ||
| - | [[Category: e | + | [[Category: e coli]] |
[[Category: heme]] | [[Category: heme]] | ||
[[Category: oxygen storage/transport]] | [[Category: oxygen storage/transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:23 2008'' |
Revision as of 12:58, 21 February 2008
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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 with and as ligands. 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 Thu Feb 21 14:58:23 2008
Categories: Escherichia coli | Single protein | Kang, C H. | Park, H J. | Satterlee, J D. | Suquet, C. | HEM | OXY | E coli | Heme | Oxygen storage/transport
