1u4h
From Proteopedia
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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 SCN, HEM, OXY and GOL 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 Sun Nov 25 03:18:05 2007
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
