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| | {{STRUCTURE_1nfp| PDB=1nfp | SCENE= }} | | {{STRUCTURE_1nfp| PDB=1nfp | SCENE= }} |
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| - | '''STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION'''
| + | ===STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_7776372}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7776372 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7776372}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Flavin mononucleotide]] | | [[Category: Flavin mononucleotide]] |
| | [[Category: Myristate]] | | [[Category: Myristate]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:28:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:44:52 2008'' |
Revision as of 16:44, 27 July 2008
Template:STRUCTURE 1nfp
STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 7776372
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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