2fc2

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[[Image:2fc2.gif|left|200px]]
 
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==NO-HEME complex in a bacterial nitric oxide synthase. An Fe(III)-NO may cause nitrosation.==
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The line below this paragraph, containing "STRUCTURE_2fc2", creates the "Structure Box" on the page.
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<StructureSection load='2fc2' size='340' side='right'caption='[[2fc2]], [[Resolution|resolution]] 2.20&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'>[[2fc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FC2 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]] 2.2&#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=HAR:N-OMEGA-HYDROXY-L-ARGININE'>HAR</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene></td></tr>
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{{STRUCTURE_2fc2| PDB=2fc2 | 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=2fc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fc2 OCA], [https://pdbe.org/2fc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fc2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fc2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NOSO_BACSU NOSO_BACSU] Catalyzes the production of nitric oxide.
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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/fc/2fc2_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=2fc2 ConSurf].
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<div style="clear:both"></div>
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'''NO-HEME complex in a bacterial nitric oxide synthase. An Fe(III)-NO may cause nitrosation.'''
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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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The crystal structures of nitrosyl-heme complexes of a prokaryotic nitric oxide synthase (NOS) from Bacillus subtilis (bsNOS) reveal changes in active-site hydrogen bonding in the presence of the intermediate N(omega)-hydroxy-l-arginine (NOHA) compared to the substrate l-arginine (l-Arg). Correlating with a Val-to-Ile residue substitution in the bsNOS heme pocket, the Fe(II)-NO complex with both l-Arg and NOHA is more bent than the Fe(II)-NO, l-Arg complex of mammalian eNOS [Li, H., Raman, C. S., Martasek, P., Masters, B. S. S., and Poulos, T. L. (2001) Biochemistry 40, 5399-5406]. Structures of the Fe(III)-NO complex with NOHA show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound NOHA. In the Fe(II)-NO complexes, the protonated NOHA N(omega) atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. In contrast, the l-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen. This difference in hydrogen bonding to the nitrosyl group by the two substrates indicates that interactions provided by NOHA may preferentially stabilize an electrophilic peroxo-heme intermediate in the second step of NOS catalysis.
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==About this Structure==
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2FC2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FC2 OCA].
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==Reference==
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Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation., Pant K, Crane BR, Biochemistry. 2006 Feb 28;45(8):2537-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16489746 16489746]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Nitric-oxide synthase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Crane BR]]
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[[Category: Crane, B R.]]
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[[Category: Pant K]]
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[[Category: Pant, K.]]
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[[Category: N-nitrosation]]
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[[Category: Nitric oxide synthase]]
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[[Category: No-heme complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:42:52 2008''
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Current revision

NO-HEME complex in a bacterial nitric oxide synthase. An Fe(III)-NO may cause nitrosation.

PDB ID 2fc2

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