1kfv

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(New page: 200px<br /><applet load="1kfv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kfv, resolution 2.55&Aring;" /> '''Crystal Structure of...)
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[[Image:1kfv.gif|left|200px]]<br /><applet load="1kfv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kfv, resolution 2.55&Aring;" />
caption="1kfv, resolution 2.55&Aring;" />
'''Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.'''<br />
'''Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.'''<br />
==Overview==
==Overview==
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The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base, excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide, range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened, purines, from oxidatively damaged DNA. The structure of a non-covalent, complex between the Lactoccocus lactis Fpg and a 1,3-propanediol (Pr), abasic site analogue-containing DNA has been solved. Through an asymmetric, interaction along the damaged strand and the intercalation of the triad, (M75/R109/F111), Fpg pushes out the Pr site from the DNA double helix, recognizing the cytosine opposite the lesion and inducing a 60 degrees, bend of the DNA. The specific recognition of this cytosine provides some, structural basis for understanding the divergence between Fpg and its, structural homologue endo nuclease VIII towards their substrate, specificities. In addition, the modelling of the 8-oxoguanine residue, allows us to define an enzyme pocket that may accommodate the extrahelical, oxidized base.
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The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened purines, from oxidatively damaged DNA. The structure of a non-covalent complex between the Lactoccocus lactis Fpg and a 1,3-propanediol (Pr) abasic site analogue-containing DNA has been solved. Through an asymmetric interaction along the damaged strand and the intercalation of the triad (M75/R109/F111), Fpg pushes out the Pr site from the DNA double helix, recognizing the cytosine opposite the lesion and inducing a 60 degrees bend of the DNA. The specific recognition of this cytosine provides some structural basis for understanding the divergence between Fpg and its structural homologue endo nuclease VIII towards their substrate specificities. In addition, the modelling of the 8-oxoguanine residue allows us to define an enzyme pocket that may accommodate the extrahelical oxidized base.
==About this Structure==
==About this Structure==
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1KFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-formamidopyrimidine_glycosylase DNA-formamidopyrimidine glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.23 3.2.2.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KFV OCA].
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1KFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-formamidopyrimidine_glycosylase DNA-formamidopyrimidine glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.23 3.2.2.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFV OCA].
==Reference==
==Reference==
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[[Category: Boiteux, S.]]
[[Category: Boiteux, S.]]
[[Category: Castaing, B.]]
[[Category: Castaing, B.]]
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[[Category: Jesus, K.Pereira.de.]]
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[[Category: Jesus, K Pereira de.]]
[[Category: Serre, L.]]
[[Category: Serre, L.]]
[[Category: Zelwer, C.]]
[[Category: Zelwer, C.]]
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[[Category: n-glycosylase]]
[[Category: n-glycosylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:10:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:41 2008''

Revision as of 11:33, 21 February 2008


1kfv, resolution 2.55Å

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Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.

Overview

The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened purines, from oxidatively damaged DNA. The structure of a non-covalent complex between the Lactoccocus lactis Fpg and a 1,3-propanediol (Pr) abasic site analogue-containing DNA has been solved. Through an asymmetric interaction along the damaged strand and the intercalation of the triad (M75/R109/F111), Fpg pushes out the Pr site from the DNA double helix, recognizing the cytosine opposite the lesion and inducing a 60 degrees bend of the DNA. The specific recognition of this cytosine provides some structural basis for understanding the divergence between Fpg and its structural homologue endo nuclease VIII towards their substrate specificities. In addition, the modelling of the 8-oxoguanine residue allows us to define an enzyme pocket that may accommodate the extrahelical oxidized base.

About this Structure

1KFV is a Single protein structure of sequence from Lactococcus lactis with and as ligands. Active as DNA-formamidopyrimidine glycosylase, with EC number 3.2.2.23 Full crystallographic information is available from OCA.

Reference

Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA., Serre L, Pereira de Jesus K, Boiteux S, Zelwer C, Castaing B, EMBO J. 2002 Jun 17;21(12):2854-65. PMID:12065399

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