1u4h

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(New page: 200px<br /><applet load="1u4h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u4h, resolution 2.07&Aring;" /> '''Crystal structure of...)
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[[Image:1u4h.gif|left|200px]]<br /><applet load="1u4h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u4h, resolution 2.07&Aring;" />
caption="1u4h, resolution 2.07&Aring;" />
'''Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)'''<br />
'''Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)'''<br />
==Overview==
==Overview==
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Soluble guanylate cyclases are nitric oxide-responsive signaling proteins, in which the nitric oxide sensor is a heme-binding domain of unknown, structure that we have termed the heme-NO and oxygen binding (H-NOX), domain. H-NOX domains are also found in bacteria, either as isolated, domains, or are fused through a membrane-spanning region to, methyl-accepting chemotaxis proteins. We have determined the crystal, structure of an oxygen-binding H-NOX domain of one such signaling protein, from the obligate anaerobe Thermoanaerobacter tengcongensis at, 1.77-angstroms resolution, revealing a protein fold unrelated to known, structures. Particularly striking is the structure of the protoporphyrin, IX group, which is distorted from planarity to an extent not seen before, in protein-bound heme groups. Comparison of the structure of the H-NOX, domain in two different crystal forms suggests a mechanism whereby, alteration in the degree of distortion of the heme group is coupled to, changes on the molecular surface of the H-NOX domain and potentially to, changes in intermolecular interactions.
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Soluble guanylate cyclases are nitric oxide-responsive signaling proteins in which the nitric oxide sensor is a heme-binding domain of unknown structure that we have termed the heme-NO and oxygen binding (H-NOX) domain. H-NOX domains are also found in bacteria, either as isolated domains, or are fused through a membrane-spanning region to methyl-accepting chemotaxis proteins. We have determined the crystal structure of an oxygen-binding H-NOX domain of one such signaling protein from the obligate anaerobe Thermoanaerobacter tengcongensis at 1.77-angstroms resolution, revealing a protein fold unrelated to known structures. Particularly striking is the structure of the protoporphyrin IX group, which is distorted from planarity to an extent not seen before in protein-bound heme groups. Comparison of the structure of the H-NOX domain in two different crystal forms suggests a mechanism whereby alteration in the degree of distortion of the heme group is coupled to changes on the molecular surface of the H-NOX domain and potentially to changes in intermolecular interactions.
==About this Structure==
==About this Structure==
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1U4H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacter_tengcongensis Thermoanaerobacter tengcongensis] with SCN, HEM, OXY and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U4H OCA].
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1U4H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacter_tengcongensis Thermoanaerobacter tengcongensis] with <scene name='pdbligand=SCN:'>SCN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U4H OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermoanaerobacter tengcongensis]]
[[Category: Thermoanaerobacter tengcongensis]]
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[[Category: Boon, E.M.]]
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[[Category: Boon, E M.]]
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[[Category: Karow, D.S.]]
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[[Category: Karow, D S.]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
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[[Category: Marletta, M.A.]]
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[[Category: Marletta, M A.]]
[[Category: Pellicena, P.]]
[[Category: Pellicena, P.]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:18:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:32 2008''

Revision as of 13:20, 21 February 2008


1u4h, resolution 2.07Å

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Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)

Overview

Soluble guanylate cyclases are nitric oxide-responsive signaling proteins in which the nitric oxide sensor is a heme-binding domain of unknown structure that we have termed the heme-NO and oxygen binding (H-NOX) domain. H-NOX domains are also found in bacteria, either as isolated domains, or are fused through a membrane-spanning region to methyl-accepting chemotaxis proteins. We have determined the crystal structure of an oxygen-binding H-NOX domain of one such signaling protein from the obligate anaerobe Thermoanaerobacter tengcongensis at 1.77-angstroms resolution, revealing a protein fold unrelated to known structures. Particularly striking is the structure of the protoporphyrin IX group, which is distorted from planarity to an extent not seen before in protein-bound heme groups. Comparison of the structure of the H-NOX domain in two different crystal forms suggests a mechanism whereby alteration in the degree of distortion of the heme group is coupled to changes on the molecular surface of the H-NOX domain and potentially to changes in intermolecular interactions.

About this Structure

1U4H is a Single protein structure of sequence from Thermoanaerobacter tengcongensis with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases., Pellicena P, Karow DS, Boon EM, Marletta MA, Kuriyan J, Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12854-9. Epub 2004 Aug 23. PMID:15326296

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