1nse
From Proteopedia
(New page: 200px<br /><applet load="1nse" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nse, resolution 1.9Å" /> '''BOVINE ENDOTHELIAL NI...) |
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| - | [[Image:1nse.gif|left|200px]]<br /><applet load="1nse" size=" | + | [[Image:1nse.gif|left|200px]]<br /><applet load="1nse" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nse, resolution 1.9Å" /> | caption="1nse, resolution 1.9Å" /> | ||
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE'''<br /> | '''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nitric oxide, a key signaling molecule, is produced by a family of enzymes | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NSE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACT, CAC, ZN, HEM, H4B, ITU and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http:// | + | 1NSE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=H4B:'>H4B</scene>, <scene name='pdbligand=ITU:'>ITU</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Li, H.]] | [[Category: Li, H.]] | ||
[[Category: Martasek, P.]] | [[Category: Martasek, P.]] | ||
| - | [[Category: Masters, B | + | [[Category: Masters, B S.S.]] |
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
| - | [[Category: Raman, C | + | [[Category: Raman, C S.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CAC]] | [[Category: CAC]] | ||
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[[Category: tetrahydrobiopterin]] | [[Category: tetrahydrobiopterin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:27 2008'' |
Revision as of 12:09, 21 February 2008
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BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
Overview
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.
About this Structure
1NSE is a Single protein structure of sequence from Bos taurus with , , , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
Reference
Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center., Raman CS, Li H, Martasek P, Kral V, Masters BS, Poulos TL, Cell. 1998 Dec 23;95(7):939-50. PMID:9875848
Page seeded by OCA on Thu Feb 21 14:09:27 2008
Categories: Bos taurus | Nitric-oxide synthase | Single protein | Kral, V. | Li, H. | Martasek, P. | Masters, B S.S. | Poulos, T L. | Raman, C S. | ACT | CAC | GOL | H4B | HEM | ITU | ZN | Arginine | Heme protein | Nitric oxide synthase | Oxidoreductase | Tetrahydrobiopterin
