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1flm

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(New page: 200px<br /><applet load="1flm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1flm, resolution 1.30&Aring;" /> '''DIMER OF FMN-BINDING...)
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[[Image:1flm.gif|left|200px]]<br /><applet load="1flm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1flm, resolution 1.30&Aring;" />
caption="1flm, resolution 1.30&Aring;" />
'''DIMER OF FMN-BINDING PROTEIN FROM DESULFOVIBRIO VULGARIS (MIYAZAKI F)'''<br />
'''DIMER OF FMN-BINDING PROTEIN FROM DESULFOVIBRIO VULGARIS (MIYAZAKI F)'''<br />
==Overview==
==Overview==
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The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio, vulgaris Miyazaki F was solved by the multiple isomorphous replacement, method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp, exists in a dimeric form in the crystal, in contrast to the monomeric, structure determined by NMR. R.m.s. deviations between the crystal, structure and the solution structure are more than 2 A, which implies, significant differences. There are some hydrophobic residues in the, interface between the two monomers. In particular, Leu122 in the, C-terminus has a close contact with the o-xylene moiety of FMN, while, solvent molecules may cover the o-xylene moiety in the solution structure.
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The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp exists in a dimeric form in the crystal, in contrast to the monomeric structure determined by NMR. R.m.s. deviations between the crystal structure and the solution structure are more than 2 A, which implies significant differences. There are some hydrophobic residues in the interface between the two monomers. In particular, Leu122 in the C-terminus has a close contact with the o-xylene moiety of FMN, while solvent molecules may cover the o-xylene moiety in the solution structure.
==About this Structure==
==About this Structure==
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1FLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FLM OCA].
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1FLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLM OCA].
==Reference==
==Reference==
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[[Category: fmn binding]]
[[Category: fmn binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:01:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:55 2008''

Revision as of 10:39, 21 February 2008


1flm, resolution 1.30Å

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DIMER OF FMN-BINDING PROTEIN FROM DESULFOVIBRIO VULGARIS (MIYAZAKI F)

Overview

The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp exists in a dimeric form in the crystal, in contrast to the monomeric structure determined by NMR. R.m.s. deviations between the crystal structure and the solution structure are more than 2 A, which implies significant differences. There are some hydrophobic residues in the interface between the two monomers. In particular, Leu122 in the C-terminus has a close contact with the o-xylene moiety of FMN, while solvent molecules may cover the o-xylene moiety in the solution structure.

About this Structure

1FLM is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. Full crystallographic information is available from OCA.

Reference

How do the x-ray structure and the NMR structure of FMN-binding protein differ?, Suto K, Kawagoe K, Shibata N, Morimoto Y, Higuchi Y, Kitamura M, Nakaya T, Yasuoka N, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):368-71. PMID:10713530

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