1nfp
From Proteopedia
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|PDB= 1nfp |SIZE=350|CAPTION= <scene name='initialview01'>1nfp</scene>, resolution 1.60Å | |PDB= 1nfp |SIZE=350|CAPTION= <scene name='initialview01'>1nfp</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nfp OCA], [http://www.ebi.ac.uk/pdbsum/1nfp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nfp RCSB]</span> | ||
}} | }} | ||
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[[Category: Moore, S A.]] | [[Category: Moore, S A.]] | ||
[[Category: Njames, M N.G.]] | [[Category: Njames, M N.G.]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: MYR]] | ||
| - | [[Category: SO4]] | ||
[[Category: flavin mononucleotide]] | [[Category: flavin mononucleotide]] | ||
[[Category: myristate]] | [[Category: myristate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:29:44 2008'' |
Revision as of 19:29, 30 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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