1u4h
From Proteopedia
(New page: 200px<br /><applet load="1u4h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u4h, resolution 2.07Å" /> '''Crystal structure of...) |
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- | [[Image:1u4h.gif|left|200px]]<br /><applet load="1u4h" size=" | + | [[Image:1u4h.gif|left|200px]]<br /><applet load="1u4h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u4h, resolution 2.07Å" /> | caption="1u4h, resolution 2.07Å" /> | ||
'''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== | ||
- | Soluble guanylate cyclases are nitric oxide-responsive signaling proteins | + | 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== | ||
- | 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:// | + | 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]] | ||
- | [[Category: Boon, E | + | [[Category: Boon, E M.]] |
- | [[Category: Karow, D | + | [[Category: Karow, D S.]] |
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
- | [[Category: Marletta, M | + | [[Category: Marletta, M A.]] |
[[Category: Pellicena, P.]] | [[Category: Pellicena, P.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
- | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 15:20:32 2008
Categories: Single protein | Thermoanaerobacter tengcongensis | Boon, E M. | Karow, D S. | Kuriyan, J. | Marletta, M A. | Pellicena, P. | GOL | HEM | OXY | SCN | Chemotaxis | H-nox domain | Heme | Oxygen sensor | Signal transduction