1U4H

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

Summary for 1U4H

• Entry DOI: 10.2210/pdb1u4h/pdb
• Related: 1U55 1U56
• Descriptor: Heme-based Methyl-accepting Chemotaxis Protein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (6 entities in total)
• Functional Keywords: h-nox domain, heme, oxygen sensor, signal transduction, chemotaxis, signaling protein
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 2
• Total formula weight: 46474.97

Authors

Pellicena, P.,Karow, D.S.,Boon, E.M.,Marletta, M.A.,Kuriyan, J. (deposition date: 2004-07-25, release date: 2004-08-31, Last modification date: 2024-11-20)

Primary citation

Pellicena, P.,Karow, D.S.,Boon, E.M.,Marletta, M.A.,Kuriyan, J.
Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.
Proc.Natl.Acad.Sci.Usa, 101:12854-12859, 2004

PubMed Abstract: 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.

PubMed: 15326296
DOI: 10.1073/pnas.0405188101

Experimental method

X-RAY DIFFRACTION (2.07 Å)