1nfp
From Proteopedia
(New page: 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=" | + | [[Image:1nfp.jpg|left|200px]]<br /><applet load="1nfp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nfp, resolution 1.60Å" /> | caption="1nfp, resolution 1.60Å" /> | ||
'''STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystallographically-determined structure of the non-fluorescent | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Photobacterium leiognathi]] | [[Category: Photobacterium leiognathi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Moore, S | + | [[Category: Moore, S A.]] |
| - | [[Category: Njames, M | + | [[Category: Njames, M N.G.]] |
[[Category: FMN]] | [[Category: FMN]] | ||
[[Category: MYR]] | [[Category: MYR]] | ||
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[[Category: myristate]] | [[Category: myristate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:36 2008'' |
Revision as of 12:05, 21 February 2008
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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 with , and as ligands. 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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