1m00

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[[Image:1m00.gif|left|200px]]
 
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==Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound==
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The line below this paragraph, containing "STRUCTURE_1m00", creates the "Structure Box" on the page.
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<StructureSection load='1m00' size='340' side='right'caption='[[1m00]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m00]] 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=1M00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M00 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#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=BHH:N-BUTYL-N-HYDROXYGUANIDINE'>BHH</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1m00| PDB=1m00 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m00 OCA], [https://pdbe.org/1m00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m00 RCSB], [https://www.ebi.ac.uk/pdbsum/1m00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m00 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m0/1m00_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1m00 ConSurf].
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<div style="clear:both"></div>
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'''Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound'''
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==See Also==
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*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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A series of N-alkyl-N'-hydroxyguanidine compounds have recently been characterized as non-amino acid substrates for all three nitric oxide synthase (NOS) isoforms which mimic NO formation from N(omega)-hydroxy-L-arginine. Crystal structures of the nNOS heme domain complexed with either N-isopropyl-N'-hydroxyguanidine or N-butyl-N'-hydroxyguanidine reveal two different binding modes in the substrate binding pocket. The binding mode of the latter is consistent with that observed for the substrate N(omega)-hydroxy-L-arginine bound in the nNOS active site. However, the former binds to nNOS in an unexpected fashion, thus providing new insights into the mechanism on how the hydroxyguanidine moiety leads to NO formation. Structural features of substrate binding support the view that the OH-substituted guanidine nitrogen, instead of the hydroxyl oxygen, is the source of hydrogen supplied to the active ferric-superoxy species for the second step of the NOS catalytic reaction.
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[[Category: Large Structures]]
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==About this Structure==
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1M00 is a [[Single protein]] structure of sequence 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=1M00 OCA].
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==Reference==
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The novel binding mode of N-alkyl-N'-hydroxyguanidine to neuronal nitric oxide synthase provides mechanistic insights into NO biosynthesis., Li H, Shimizu H, Flinspach M, Jamal J, Yang W, Xian M, Cai T, Wen EZ, Jia Q, Wang PG, Poulos TL, Biochemistry. 2002 Nov 26;41(47):13868-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12437343 12437343]
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[[Category: Nitric-oxide synthase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Cai T]]
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[[Category: Cai, T.]]
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[[Category: Flinspach M]]
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[[Category: Flinspach, M.]]
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[[Category: Jamal J]]
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[[Category: Jamal, J.]]
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[[Category: Jia Q]]
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[[Category: Jia, Q.]]
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[[Category: Li H]]
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[[Category: Li, H.]]
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[[Category: Poulos TL]]
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[[Category: Poulos, T L.]]
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[[Category: Shimizu H]]
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[[Category: Shimizu, H.]]
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[[Category: Wang PG]]
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[[Category: Wang, P G.]]
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[[Category: Wen EZ]]
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[[Category: Wen, E Z.]]
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[[Category: Xian M]]
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[[Category: Xian, M.]]
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[[Category: Yang W]]
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[[Category: Yang, W.]]
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[[Category: Heme-enzyme]]
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[[Category: Nitric oxide synthase]]
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[[Category: Oxydoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:28:04 2008''
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Current revision

Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound

PDB ID 1m00

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