Unknown

Dataset Information

0

Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.


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.

SUBMITTER: Pellicena P 

PROVIDER: S-EPMC516465 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.

Pellicena Patricia P   Karow David S DS   Boon Elizabeth M EM   Marletta Michael A MA   Kuriyan John J  

Proceedings of the National Academy of Sciences of the United States of America 20040823 35


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 obligat  ...[more]

Similar Datasets

| S-EPMC8640258 | biostudies-literature
| S-EPMC3091176 | biostudies-literature
| S-EPMC3591389 | biostudies-literature
| S-EPMC4932850 | biostudies-literature
| S-EPMC3430480 | biostudies-literature
| S-EPMC2760494 | biostudies-literature
| S-EPMC2014653 | biostudies-other
| S-EPMC3096724 | biostudies-literature
| S-EPMC2576301 | biostudies-literature
| S-EPMC4032937 | biostudies-literature