1U56

Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (Water-ligated, ferric form)

Summary for 1U56

• Entry DOI: 10.2210/pdb1u56/pdb
• Related: 1U4H 1U55
• Descriptor: Heme-based Methyl-accepting chemotaxis protein, PROTOPORPHYRIN IX CONTAINING FE, CHLORIDE ION, ... (4 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: 45363.43

Authors

Pellicena, P.,Karow, D.S.,Boon, E.M.,Marletta, M.A.,Kuriyan, J. (deposition date: 2004-07-27, release date: 2004-08-31, Last modification date: 2023-08-23)

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 (1.9 Å)