1zfn

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(New page: 200px<br /><applet load="1zfn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zfn, resolution 2.75&Aring;" /> '''Structural Analysis ...)
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[[Image:1zfn.gif|left|200px]]<br /><applet load="1zfn" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zfn.gif|left|200px]]<br /><applet load="1zfn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zfn, resolution 2.75&Aring;" />
caption="1zfn, resolution 2.75&Aring;" />
'''Structural Analysis of Escherichia coli ThiF'''<br />
'''Structural Analysis of Escherichia coli ThiF'''<br />
==Overview==
==Overview==
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Escherichia coli ThiF is an enzyme in the biosynthetic cascade for, generating the essential cofactor thiamin pyrophosphate. In this cascade, ThiF catalyzes adenylation of the C terminus of ThiS. We report here the, crystal structures of ThiF, alone and in complex with ATP. The structures, provide insight into a preference for ATP during adenylation of the, protein ThiS. Additionally, the structures reveal an ordered crossover, loop predicted to clamp the flexible tail of ThiS into the ThiF active, site during the adenylation reaction. The importance of the crossover loop, for ThiF activity is highlighted by mutational analysis. Comparison of, ThiF with the structural homologues MoeB, APPBP1-UBA3, and SAE1-SAE2, reveals that the ATP-binding site, including an arginine-finger, is, maintained throughout evolution, and shows divergence occurring in protein, substrate-binding sites and regions devoted to unique steps in the, specific function of each enzyme.
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Escherichia coli ThiF is an enzyme in the biosynthetic cascade for generating the essential cofactor thiamin pyrophosphate. In this cascade, ThiF catalyzes adenylation of the C terminus of ThiS. We report here the crystal structures of ThiF, alone and in complex with ATP. The structures provide insight into a preference for ATP during adenylation of the protein ThiS. Additionally, the structures reveal an ordered crossover loop predicted to clamp the flexible tail of ThiS into the ThiF active site during the adenylation reaction. The importance of the crossover loop for ThiF activity is highlighted by mutational analysis. Comparison of ThiF with the structural homologues MoeB, APPBP1-UBA3, and SAE1-SAE2 reveals that the ATP-binding site, including an arginine-finger, is maintained throughout evolution, and shows divergence occurring in protein substrate-binding sites and regions devoted to unique steps in the specific function of each enzyme.
==About this Structure==
==About this Structure==
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1ZFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZFN OCA].
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1ZFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFN OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Duda, D.M.]]
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[[Category: Duda, D M.]]
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[[Category: Schulman, B.A.]]
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[[Category: Schulman, B A.]]
[[Category: Sfondouris, J.]]
[[Category: Sfondouris, J.]]
[[Category: Walden, H.]]
[[Category: Walden, H.]]
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[[Category: this]]
[[Category: this]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:25:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:04 2008''

Revision as of 14:15, 21 February 2008

Image:1zfn.gif

1zfn, resolution 2.75Å

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Structural Analysis of Escherichia coli ThiF

Overview

Escherichia coli ThiF is an enzyme in the biosynthetic cascade for generating the essential cofactor thiamin pyrophosphate. In this cascade, ThiF catalyzes adenylation of the C terminus of ThiS. We report here the crystal structures of ThiF, alone and in complex with ATP. The structures provide insight into a preference for ATP during adenylation of the protein ThiS. Additionally, the structures reveal an ordered crossover loop predicted to clamp the flexible tail of ThiS into the ThiF active site during the adenylation reaction. The importance of the crossover loop for ThiF activity is highlighted by mutational analysis. Comparison of ThiF with the structural homologues MoeB, APPBP1-UBA3, and SAE1-SAE2 reveals that the ATP-binding site, including an arginine-finger, is maintained throughout evolution, and shows divergence occurring in protein substrate-binding sites and regions devoted to unique steps in the specific function of each enzyme.

About this Structure

1ZFN is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural analysis of Escherichia coli ThiF., Duda DM, Walden H, Sfondouris J, Schulman BA, J Mol Biol. 2005 Jun 17;349(4):774-86. PMID:15896804

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