2all: Difference between revisions
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|PDB= 2all |SIZE=350|CAPTION= <scene name='initialview01'>2all</scene>, resolution 1.47Å | |PDB= 2all |SIZE=350|CAPTION= <scene name='initialview01'>2all</scene>, resolution 1.47Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2a3f|2A3F]], [[1pm1|1PM1]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2all FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2all OCA], [http://www.ebi.ac.uk/pdbsum/2all PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2all RCSB]</span> | |||
}} | }} | ||
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[[Category: Walker, F A.]] | [[Category: Walker, F A.]] | ||
[[Category: Weichsel, A.]] | [[Category: Weichsel, A.]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: double mutant]] | [[Category: double mutant]] | ||
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[[Category: lipocalin]] | [[Category: lipocalin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:54:15 2008'' | ||
Revision as of 01:54, 31 March 2008
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| , resolution 1.47Å | |||||||
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| Ligands: | |||||||
| Related: | 2A3F, 1PM1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of L122V/L132V mutant of nitrophorin 2
OverviewOverview
Nitrophorin 2 (NP2) (also known as prolixin-S) is a salivary protein that transports nitric oxide, binds histamine, and acts as an anticoagulant during blood feeding by the insect Rhodnius prolixus. The 2.0-A crystal structure of NP2 reveals an eight-stranded antiparallel beta-barrel containing a ferric heme coordinated through His(57), similar to the structures of NP1 and NP4. All four Rhodnius nitrophorins transport NO and sequester histamine through heme binding, but only NP2 acts as an anticoagulant. Here, we demonstrate that recombinant NP2, but not recombinant NP1 or NP4, is a potent anticoagulant; recombinant NP3 also displays minor activity. Comparison of the nitrophorin structures suggests that a surface region near the C terminus and the loops between beta strands B-C and E-F is responsible for the anticoagulant activity. NP2 also displays larger NO association rates and smaller dissociation rates than NP1 and NP4, which may result from a more open and more hydrophobic distal pocket, allowing more rapid solvent reorganization on ligand binding. The NP2 protein core differs from NP1 and NP4 in that buried Glu(53), which allows for larger NO release rates when deprotonated, hydrogen bonds to invariant Tyr(81). Surprisingly, this tyrosine lies on the protein surface in NP1 and NP4.
About this StructureAbout this Structure
2ALL is a Single protein structure of sequence from Rhodnius prolixus. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of nitrophorin 2. A trifunctional antihemostatic protein from the saliva of Rhodnius prolixus., Andersen JF, Montfort WR, J Biol Chem. 2000 Sep 29;275(39):30496-503. PMID:10884386
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