1D3S
1.4 A crystal structure of nitrophorin 4 from Rhodnius prolixis at pH=5.6.
Summary for 1D3S
| Entry DOI | 10.2210/pdb1d3s/pdb |
| Related | 1D2U 1NP4 |
| Descriptor | NITROPHORIN 4, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | nitric oxide transport, ferric heme, antihistamine, vasodilator, lipocalin, transport protein |
| Biological source | Rhodnius prolixus |
| Cellular location | Secreted: Q94734 |
| Total number of polymer chains | 1 |
| Total formula weight | 20909.15 |
| Authors | Weichsel, A.,Andersen, J.F.,Roberts, S.A.,Montfort, W.R. (deposition date: 1999-09-30, release date: 2000-07-07, Last modification date: 2024-10-30) |
| Primary citation | Weichsel, A.,Andersen, J.F.,Roberts, S.A.,Montfort, W.R. Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial. Nat.Struct.Biol., 7:551-554, 2000 Cited by PubMed 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. PubMed: 10876239DOI: 10.1038/76769 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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