1fvp
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(New page: 200px<br /><applet load="1fvp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvp, resolution 2.7Å" /> '''FLAVOPROTEIN 390'''<b...)
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Revision as of 13:13, 20 November 2007
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FLAVOPROTEIN 390
Overview
The three-dimensional structure of a flavoprotein, FP(390), from a, luminescent bacterium, Photobacterium phosphoreum, solved by the, molecular-replacement method, was refined to an R factor of 24.0% for 17, 433 independent reflections, from 6.0 to 2.7 A resolution, collected by, synchrotron radiation. The asymmetric unit of the crystal (space group, P4(3)22, a = b = 76.8 and c = 242 A) contains two monomer molecules, related by a non-crystallographic twofold axis to form a dimer. There are, two Q-flavin [flavin mononucleotide (FMN) with myristic acid] molecules in, FP(390) monomer. One of them is located at the interface of dimer which is, bound to both monomer and the another is at the molecular surface. The, electron density of myristic acids of Q-flavins at the dimer interface in, both monomer are weak and unclear, showing the possibility that the, Q-flavins bound in this site are not a single species but a mixture of two, components, 6-(3"-myristic acid)-FMN and 6-(4"- myristic acid)-FMN.
About this Structure
1FVP is a Single protein structure of sequence from Photobacterium phosphoreum with FMA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of flavoprotein FP390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 A resolution., Kita A, Kasai S, Miyata M, Miki K, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):77-86. PMID:15299728
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