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 2.7&Aring;" /> '''FLAVOPROTEIN 390'''<b...)
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[[Image:1fvp.gif|left|200px]]<br /><applet load="1fvp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fvp, resolution 2.7&Aring;" />
caption="1fvp, resolution 2.7&Aring;" />
'''FLAVOPROTEIN 390'''<br />
'''FLAVOPROTEIN 390'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1FVP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_phosphoreum Photobacterium phosphoreum] with FMA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FVP OCA].
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1FVP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_phosphoreum Photobacterium phosphoreum] with <scene name='pdbligand=FMA:'>FMA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVP OCA].
==Reference==
==Reference==
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[[Category: flavin-binding protein]]
[[Category: flavin-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:20:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:06 2008''

Revision as of 10:43, 21 February 2008


1fvp, resolution 2.7Å

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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 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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