1nfp

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[[Image:1nfp.jpg|left|200px]]<br /><applet load="1nfp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nfp.jpg|left|200px]]
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caption="1nfp, resolution 1.60&Aring;" />
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'''STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1nfp |SIZE=350|CAPTION= <scene name='initialview01'>1nfp</scene>, resolution 1.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=MYR:MYRISTIC ACID'>MYR</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFP OCA].
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1NFP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFP OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/7776372 7776372]
[[Category: Photobacterium leiognathi]]
[[Category: Photobacterium leiognathi]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: myristate]]
[[Category: myristate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:56:15 2008''

Revision as of 10:56, 20 March 2008


PDB ID 1nfp

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1NFP is a Single protein structure of sequence from Photobacterium leiognathi. Full crystallographic information is available from OCA.

Reference

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:7776372

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