1u56: Difference between revisions
New page: left|200px<br /><applet load="1u56" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u56, resolution 1.90Å" /> '''Crystal structure of... |
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[[Image:1u56.gif|left|200px]]<br /><applet load="1u56" size=" | [[Image:1u56.gif|left|200px]]<br /><applet load="1u56" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1u56, resolution 1.90Å" /> | caption="1u56, resolution 1.90Å" /> | ||
'''Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (Water-ligated, ferric form)'''<br /> | '''Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (Water-ligated, ferric form)'''<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== | ||
1U56 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 CL and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1U56 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=CL:'>CL</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U56 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: CL]] | [[Category: CL]] | ||
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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 15:20:44 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 (Water-ligated, ferric form)
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
1U56 is a Single protein structure of sequence from Thermoanaerobacter tengcongensis with CL and HEM 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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