1drm

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(New page: 200px<br /><applet load="1drm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1drm, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN'''<br />
'''CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN'''<br />
==Overview==
==Overview==
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The FixL proteins are biological oxygen sensors that restrict the, expression of specific genes to hypoxic conditions. FixL's, oxygen-detecting domain is a heme binding region that controls the, activity of an attached histidine kinase. The FixL switch is regulated by, binding of oxygen and other strong-field ligands. In the absence of bound, ligand, the heme domain permits kinase activity. In the presence of bound, ligand, this domain turns off kinase activity. Comparison of the, structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with, bound cyanide, reveals a mechanism of regulation by a heme that is, distinct from the classical hemoglobin models. The close structural, resemblance of the FixL heme domain to the photoactive yellow protein, confirms the existence of a PAS structural motif but reveals the presence, of an alternative regulatory gateway.
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The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity. Comparison of the structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with bound cyanide, reveals a mechanism of regulation by a heme that is distinct from the classical hemoglobin models. The close structural resemblance of the FixL heme domain to the photoactive yellow protein confirms the existence of a PAS structural motif but reveals the presence of an alternative regulatory gateway.
==About this Structure==
==About this Structure==
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1DRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1BV6. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DRM OCA].
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1DRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1BV6. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRM OCA].
==Reference==
==Reference==
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[[Category: Bradyrhizobium japonicum]]
[[Category: Bradyrhizobium japonicum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chan, M.K.]]
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[[Category: Chan, M K.]]
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[[Category: Gilles-Gonzalez, M.A.]]
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[[Category: Gilles-Gonzalez, M A.]]
[[Category: Gong, W.]]
[[Category: Gong, W.]]
[[Category: Gonzalez, G.]]
[[Category: Gonzalez, G.]]
[[Category: Hao, B.]]
[[Category: Hao, B.]]
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[[Category: Mansy, S.S.]]
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[[Category: Mansy, S S.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: crystal structure]]
[[Category: crystal structure]]
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[[Category: two-component system]]
[[Category: two-component system]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:31:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:42 2008''

Revision as of 10:19, 21 February 2008


1drm, resolution 2.40Å

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CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN

Overview

The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity. Comparison of the structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with bound cyanide, reveals a mechanism of regulation by a heme that is distinct from the classical hemoglobin models. The close structural resemblance of the FixL heme domain to the photoactive yellow protein confirms the existence of a PAS structural motif but reveals the presence of an alternative regulatory gateway.

About this Structure

1DRM is a Single protein structure of sequence from Bradyrhizobium japonicum with as ligand. This structure supersedes the now removed PDB entry 1BV6. Full crystallographic information is available from OCA.

Reference

Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction., Gong W, Hao B, Mansy SS, Gonzalez G, Gilles-Gonzalez MA, Chan MK, Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15177-82. PMID:9860942

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