3hso: Difference between revisions

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{{Seed}}
[[Image:3hso.png|left|200px]]


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==Ternary structure of neuronal nitric oxide synthase with NHA and NO bound(1)==
The line below this paragraph, containing "STRUCTURE_3hso", creates the "Structure Box" on the page.
<StructureSection load='3hso' size='340' side='right'caption='[[3hso]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3hso]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HSO FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HAR:N-OMEGA-HYDROXY-L-ARGININE'>HAR</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_3hso|  PDB=3hso  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hso OCA], [https://pdbe.org/3hso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hso RCSB], [https://www.ebi.ac.uk/pdbsum/3hso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hso ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOS1_RAT NOS1_RAT] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hs/3hso_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hso ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The X-ray structures of neuronal nitric oxide synthase (nNOS) with N(omega)-hydroxy-l-arginine (l-NHA) and CO (or NO) bound have been determined at 1.91-2.2 A resolution. Microspectrophotometric techniques confirmed reduced redox state and the status of diatomic ligand complexes during X-ray diffraction data collection. The structure of nNOS-NHA-NO, a close mimic to the dioxygen complex, provides a picture of the potential interactions between the heme-bound diatomic ligand, substrate l-NHA, and the surrounding protein and solvent structure environment. The OH group of l-NHA in the X-ray structures deviates from the plane of the guanidinium moiety substantially, indicating that the OH-bearing, protonated guanidine N(omega) nitrogen of l-NHA has substantial sp(3) hybridization character. This nitrogen geometry, different from that of the guanidinium N(omega) nitrogen of l-arginine, allows a hydrogen bond to be donated to the proximal oxygen of the heme-bound dioxygen complex, thus preventing cleavage of the O-O bond. Instead, it favors the stabilization of the ferric-hydroperoxy intermediate, Fe(3+)-OOH(-), which serves as the active oxidant in the conversion of l-NHA to NO and citrulline in the second reaction of the NOS.


===Ternary structure of neuronal nitric oxide synthase with NHA and NO bound(1)===
Single Crystal Structural and Absorption Spectral Characterizations of Nitric Oxide Synthase Complexed with N(omega)-Hydroxy-l-arginine and Diatomic Ligands (,).,Doukov T, Li H, Soltis M, Poulos TL Biochemistry. 2009 Oct 9. PMID:19791770<ref>PMID:19791770</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hso" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19791770}}, adds the Publication Abstract to the page
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19791770 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19791770}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3HSO is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HSO OCA].
 
==Reference==
<ref group="xtra">PMID:19791770</ref><references group="xtra"/>
[[Category: Nitric-oxide synthase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Doukov, T.]]
[[Category: Doukov T]]
[[Category: Li, H.]]
[[Category: Li H]]
[[Category: Poulos, T L.]]
[[Category: Poulos TL]]
[[Category: Soltis, M.]]
[[Category: Soltis M]]
[[Category: Alternative splicing]]
[[Category: Calmodulin-binding]]
[[Category: Cell membrane]]
[[Category: Cell projection]]
[[Category: Fad]]
[[Category: Fmn]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Nadp]]
[[Category: Nitric oxide synthase heme enzyme diatomic ligand]]
[[Category: Oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 18 17:40:00 2009''
Retrieved from "https://proteopedia.org/3hso"