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New page: left|200px<br /><applet load="1nfp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nfp, resolution 1.60Å" /> '''STRUCTURAL REFINEMEN...
 
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[[Image:1nfp.jpg|left|200px]]<br /><applet load="1nfp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1nfp, resolution 1.60&Aring;" />
'''STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION'''<br />


==Overview==
==STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION==
The crystallographically-determined structure of the non-fluorescent, flavoprotein (NFP) from Photobacterium leiognathi, a homolog of the, bacterial luciferase subunits, has been refined to a conventional R-factor, [formula: see text] of 0.175 using synchrotron data between 10.0 and 1.60, A resolution. The molecular structure is a homodimer of beta/alpha, domains, the monomer having structural similarities to (beta alpha)8, barrel proteins. However, one beta-strand and three alpha-helices of a, typical (beta alpha)8 domain are not present in the NFP structure. The, refined structure of NFP consists of the 228 amino acid polypeptide, 191, water molecules, a sulfate ion, and two flavin mononucleotides (FMNs) each, with a covalently-attached myristate (C14 fatty acid). Both flavin adducts, are well-ordered and have exceptional electron density for both the FMN, and the myristate moieties. Each flavin mononucleotide-myristate adduct is, characterized by a stereospecific linkage (the S enantiomer) between C-6, of the flavin isoalloxazine ring and the C-3' atom of the fatty acyl, chain. The stereospecific nature of this flavin-fatty acid linkage, suggests that it is the result of an enzyme-catalyzed reaction, most, likely the bioluminescence reaction itself. The myristate chains are, buried from solvent in hydrophobic pockets in the interior of the protein., Four amino acid side-chains of the NFP polypeptide have been modeled with, alternate conformations. Five of the protein's seven alpha-helices have, classical C-capping boxes. NFP is dimeric and many of the extensive, contacts at the dimer interface are mediated by hydrogen-bonded water, molecules as well as by hydrophobic interactions. One of the myristate, acyl chains sits between NFP monomers and contributes a significant, portion of the hydrophobic interactions at the NFP dimer interface.
<StructureSection load='1nfp' size='340' side='right'caption='[[1nfp]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1nfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_leiognathi_subsp._leiognathi Photobacterium leiognathi subsp. leiognathi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NFP FirstGlance]. <br>
1NFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi] with SO4, FMN and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NFP OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nfp OCA], [https://pdbe.org/1nfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nfp RCSB], [https://www.ebi.ac.uk/pdbsum/1nfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nfp ProSAT]</span></td></tr>
Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution., Moore SA, James MN, J Mol Biol. 1995 May 26;249(1):195-214. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7776372 7776372]
</table>
[[Category: Photobacterium leiognathi]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/LUXF_PHOLE LUXF_PHOLE]  
[[Category: Moore, S.A.]]
== Evolutionary Conservation ==
[[Category: Njames, M.N.G.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: FMN]]
Check<jmol>
[[Category: MYR]]
  <jmolCheckbox>
[[Category: SO4]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nf/1nfp_consurf.spt"</scriptWhenChecked>
[[Category: flavin mononucleotide]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: myristate]]
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:13:03 2007''
</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=1nfp ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Photobacterium leiognathi subsp. leiognathi]]
[[Category: Moore SA]]
[[Category: Njames MNG]]

Latest revision as of 07:56, 14 February 2024

STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION

1nfp, resolution 1.60Å

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