1buw: Difference between revisions
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|PDB= 1buw |SIZE=350|CAPTION= <scene name='initialview01'>1buw</scene>, resolution 1.9Å | |PDB= 1buw |SIZE=350|CAPTION= <scene name='initialview01'>1buw</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1buw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buw OCA], [http://www.ebi.ac.uk/pdbsum/1buw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1buw RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin. | Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Chan, N L.]] | [[Category: Chan, N L.]] | ||
[[Category: Rogers, P H.]] | [[Category: Rogers, P H.]] | ||
[[Category: oxygen transport and vasodilation]] | [[Category: oxygen transport and vasodilation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:47 2008'' | ||