Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.4
Classification:TRANSPORT PROTEIN
Release Date:2000-07-07
Deposition Date:1999-09-30
Revision Date:2008-04-27#2011-07-13#2014-10-29#2017-10-04
Molecular Weight:20909.15
Macromolecule Type:Protein
Residue Count:184
Atom Site Count:1515
DOI:10.2210/pdb1d3s/pdb
Abstract:
The nitrophorins comprise an unusual family of proteins that use ferric (Fe(III)) heme to transport highly reactive nitric oxide (NO) from the salivary gland of a blood sucking bug to the victim, resulting in vasodilation and reduced blood coagulation. We have determined structures of nitrophorin 4 in complexes with H2O, cyanide and nitric oxide. These structures reveal a remarkable feature: the nitrophorins have a broadly open distal pocket in the absence of NO, but upon NO binding, three or more water molecules are expelled and two loops fold into the distal pocket, resulting in the packing of hydrophobic groups around the NO molecule and increased distortion of the heme. In this way, the protein apparently forms a 'hydrophobic trap' for the NO molecule. The structures are very accurate, ranging between 1.6 and 1.4 A resolutions.
Resolution:1.4
Classification:TRANSPORT PROTEIN
Release Date:2000-07-07
Deposition Date:1999-09-30
Revision Date:2008-04-27#2011-07-13#2014-10-29#2017-10-04
Molecular Weight:20909.15
Macromolecule Type:Protein
Residue Count:184
Atom Site Count:1515
DOI:10.2210/pdb1d3s/pdb
Abstract:
The nitrophorins comprise an unusual family of proteins that use ferric (Fe(III)) heme to transport highly reactive nitric oxide (NO) from the salivary gland of a blood sucking bug to the victim, resulting in vasodilation and reduced blood coagulation. We have determined structures of nitrophorin 4 in complexes with H2O, cyanide and nitric oxide. These structures reveal a remarkable feature: the nitrophorins have a broadly open distal pocket in the absence of NO, but upon NO binding, three or more water molecules are expelled and two loops fold into the distal pocket, resulting in the packing of hydrophobic groups around the NO molecule and increased distortion of the heme. In this way, the protein apparently forms a 'hydrophobic trap' for the NO molecule. The structures are very accurate, ranging between 1.6 and 1.4 A resolutions.
| Date made available | 2000 |
|---|---|
| Publisher | RCSB-PDB |