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4nse

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(New page: 200px<br /><applet load="4nse" size="450" color="white" frame="true" align="right" spinBox="true" caption="4nse, resolution 1.95&Aring;" /> '''BOVINE ENDOTHELIAL N...)
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[[Image:4nse.jpg|left|200px]]<br /><applet load="4nse" size="350" color="white" frame="true" align="right" spinBox="true"
caption="4nse, resolution 1.95&Aring;" />
caption="4nse, resolution 1.95&Aring;" />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE, H4B-FREE, L-ARG COMPLEX'''<br />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE, H4B-FREE, L-ARG COMPLEX'''<br />
==Overview==
==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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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==
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4NSE 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, ARG, HEM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=4NSE OCA].
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4NSE 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=ARG:'>ARG</scene>, <scene name='pdbligand=HEM:'>HEM</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=4NSE OCA].
==Reference==
==Reference==
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[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: Martasek, P.]]
[[Category: Martasek, P.]]
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[[Category: Masters, B.S.S.]]
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[[Category: Masters, B S.S.]]
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[[Category: Poulos, T.L.]]
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[[Category: Poulos, T L.]]
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[[Category: Raman, C.S.]]
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[[Category: Raman, C S.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: ARG]]
[[Category: ARG]]
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[[Category: tetrahydrobiopterin]]
[[Category: tetrahydrobiopterin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:44:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:55 2008''

Revision as of 17:13, 21 February 2008


4nse, resolution 1.95Å

Drag the structure with the mouse to rotate

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

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

4NSE 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

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