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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 551-554 |
| Number of pages | 4 |
| Journal | Nature Structural Biology |
| Volume | 7 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 2000 |
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ASJC Scopus subject areas
- Biochemistry
- Structural Biology
- Genetics
Cite this
Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial. / Weichsel, Andrzej; Andersen, John F.; Roberts, Sue A; Montfort, William "Bill".
In: Nature Structural Biology, Vol. 7, No. 7, 07.2000, p. 551-554.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial
AU - Weichsel, Andrzej
AU - Andersen, John F.
AU - Roberts, Sue A
AU - Montfort, William "Bill"
PY - 2000/7
Y1 - 2000/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033918403&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033918403&partnerID=8YFLogxK
U2 - 10.1038/76769
DO - 10.1038/76769
M3 - Article
C2 - 10876239
AN - SCOPUS:0033918403
VL - 7
SP - 551
EP - 554
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 7
ER -