1f20
From Proteopedia
(New page: 200px<br /><applet load="1f20" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f20, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1f20.gif|left|200px]]<br /><applet load="1f20" size=" | + | [[Image:1f20.gif|left|200px]]<br /><applet load="1f20" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f20, resolution 1.9Å" /> | caption="1f20, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.'''<br /> | '''CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nitric-oxide synthase (NOS) is composed of a C-terminal, flavin-containing | + | Nitric-oxide synthase (NOS) is composed of a C-terminal, flavin-containing reductase domain and an N-terminal, heme-containing oxidase domain. The reductase domain, similar to NADPH-cytochrome P450 reductase, can be further divided into two different flavin-containing domains: (a) the N terminus, FMN-containing portion, and (b) the C terminus FAD- and NADPH-binding portion. The crystal structure of the FAD/NADPH-containing domain of rat neuronal nitric-oxide synthase, complexed with NADP(+), has been determined at 1.9 A resolution. The protein is fully capable of reducing ferricyanide, using NADPH as the electron donor. The overall polypeptide fold of the domain is very similar to that of the corresponding module of NADPH-cytochrome P450 oxidoreductase (CYPOR) and consists of three structural subdomains (from N to C termini): (a) the connecting domain, (b) the FAD-binding domain, and (c) the NADPH-binding domain. A comparison of the structure of the neuronal NOS FAD/NADPH domain and CYPOR reveals the strict conservation of the flavin-binding site, including the tightly bound water molecules, the mode of NADP(+) binding, and the aromatic residue that lies at the re-face of the flavin ring, strongly suggesting that the hydride transfer mechanisms in the two enzymes are very similar. In contrast, the putative FMN domain-binding surface of the NOS protein is less positively charged than that of its CYPOR counterpart, indicating a different nature of interactions between the two flavin domains and a different mode of regulation in electron transfer between the two flavins involving the autoinhibitory element and the C-terminal 33 residues, both of which are absent in CYPOR. |
==About this Structure== | ==About this Structure== | ||
| - | 1F20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with FAD, NAP, GOL and FMT 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:// | + | 1F20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=NAP:'>NAP</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=FMT:'>FMT</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=1F20 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kim, J | + | [[Category: Kim, J P.]] |
[[Category: Martasek, P.]] | [[Category: Martasek, P.]] | ||
| - | [[Category: Masters, B | + | [[Category: Masters, B S.]] |
[[Category: Zhang, J.]] | [[Category: Zhang, J.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: reductase domain]] | [[Category: reductase domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:54 2008'' |
Revision as of 10:34, 21 February 2008
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CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.
Overview
Nitric-oxide synthase (NOS) is composed of a C-terminal, flavin-containing reductase domain and an N-terminal, heme-containing oxidase domain. The reductase domain, similar to NADPH-cytochrome P450 reductase, can be further divided into two different flavin-containing domains: (a) the N terminus, FMN-containing portion, and (b) the C terminus FAD- and NADPH-binding portion. The crystal structure of the FAD/NADPH-containing domain of rat neuronal nitric-oxide synthase, complexed with NADP(+), has been determined at 1.9 A resolution. The protein is fully capable of reducing ferricyanide, using NADPH as the electron donor. The overall polypeptide fold of the domain is very similar to that of the corresponding module of NADPH-cytochrome P450 oxidoreductase (CYPOR) and consists of three structural subdomains (from N to C termini): (a) the connecting domain, (b) the FAD-binding domain, and (c) the NADPH-binding domain. A comparison of the structure of the neuronal NOS FAD/NADPH domain and CYPOR reveals the strict conservation of the flavin-binding site, including the tightly bound water molecules, the mode of NADP(+) binding, and the aromatic residue that lies at the re-face of the flavin ring, strongly suggesting that the hydride transfer mechanisms in the two enzymes are very similar. In contrast, the putative FMN domain-binding surface of the NOS protein is less positively charged than that of its CYPOR counterpart, indicating a different nature of interactions between the two flavin domains and a different mode of regulation in electron transfer between the two flavins involving the autoinhibitory element and the C-terminal 33 residues, both of which are absent in CYPOR.
About this Structure
1F20 is a Single protein structure of sequence from Rattus norvegicus 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 the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase., Zhang J, Martasek P, Paschke R, Shea T, Siler Masters BS, Kim JJ, J Biol Chem. 2001 Oct 5;276(40):37506-13. Epub 2001 Jul 25. PMID:11473123
Page seeded by OCA on Thu Feb 21 12:33:54 2008
Categories: Nitric-oxide synthase | Rattus norvegicus | Single protein | Kim, J P. | Martasek, P. | Masters, B S. | Zhang, J. | FAD | FMT | GOL | NAP | Fad | Nadp+ | Nitric-xoide synthase | Reductase domain
