Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NP1

CRYSTAL STRUCTURE OF THE COMPLEX OF NITROPHORIN 1 FROM RHODNIUS PROLIXUS WITH HISTAMINE

Summary for 1NP1
Entry DOI10.2210/pdb1np1/pdb
DescriptorNITROPHORIN 1, PHOSPHATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
Functional Keywordsnitric oxide transport, ferric heme, histamine, antihistamine, vasodilator, lipocalin
Biological sourceRhodnius prolixus
Cellular locationSecreted: Q26239
Total number of polymer chains2
Total formula weight42666.94
Authors
Weichsel, A.,Montfort, W.R. (deposition date: 1998-01-19, release date: 1998-05-27, Last modification date: 2024-10-30)
Primary citationWeichsel, A.,Andersen, J.F.,Champagne, D.E.,Walker, F.A.,Montfort, W.R.
Crystal structures of a nitric oxide transport protein from a blood-sucking insect.
Nat.Struct.Biol., 5:304-309, 1998
Cited by
PubMed Abstract: The nitrophorins are heme-based proteins from the salivary glands of the blood-sucking insect Rhodnius prolixus that deliver nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. The nitrophorins also bind tightly to histamine, which is released by the host to induce wound healing. Here we present three crystal structures of nitrophorin 1 (NP1): bound to cyanide, which binds in a manner similar to NO (2.3 A resolution); bound to histamine (2.0 A resolution); and bound to what appears to be NH3 from the crystallization solution (2.0 A resolution). The NP1 structures reveal heme to be sandwiched between strands of a lipocalin-like beta-barrel, and in an arrangement unlike any other gas-transport protein discovered to date. The heme is six-coordinate with a histidine (His 59) on the proximal side, and ligand in a spacious pocket on the distal side. The structures confirm that NO and histamine compete for the same binding pocket and become buried on binding. The dissociation constant for histamine binding was found to be 19 nM, approximately 100-fold lower than that for NO.
PubMed: 9546222
DOI: 10.1038/nsb0498-304
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

227111

건을2024-11-06부터공개중

PDB statisticsPDBj update infoContact PDBjnumon