4nse: Difference between revisions

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[[Image:4nse.jpg|left|200px]]
{{Seed}}
[[Image:4nse.png|left|200px]]


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{{STRUCTURE_4nse|  PDB=4nse  |  SCENE=  }}  
{{STRUCTURE_4nse|  PDB=4nse  |  SCENE=  }}  


'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE, H4B-FREE, L-ARG COMPLEX'''
===BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE, H4B-FREE, L-ARG COMPLEX===




==Overview==
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Nitric oxide, a key signaling molecule, is produced by a family of enzymes collectively called nitric oxide synthases (NOS). Here, we report the crystal structure of the heme domain of endothelial NOS in tetrahydrobiopterin (H4B)-free and -bound forms at 1.95 A and 1.9 A resolution, respectively. In both structures a zinc ion is tetrahedrally coordinated to pairs of symmetry-related cysteine residues at the dimer interface. The phylogenetically conserved Cys-(X)4-Cys motif and its strategic location establish a structural role for the metal center in maintaining the integrity of the H4B-binding site. The unexpected recognition of the substrate, L-arginine, at the H4B site indicates that this site is poised to stabilize a positively charged pterin ring and suggests a model involving a cationic pterin radical in the catalytic cycle.
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{{ABSTRACT_PUBMED_9875848}}


==About this Structure==
==About this Structure==
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[[Category: Nitric oxide synthase]]
[[Category: Nitric oxide synthase]]
[[Category: Tetrahydrobiopterin]]
[[Category: Tetrahydrobiopterin]]
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