1k82

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1k82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k82, resolution 2.10&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:1k82.gif|left|200px]]<br /><applet load="1k82" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1k82.gif|left|200px]]<br /><applet load="1k82" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k82, resolution 2.10&Aring;" />
caption="1k82, resolution 2.10&Aring;" />
'''Crystal structure of E.coli formamidopyrimidine-DNA glycosylase (Fpg) covalently trapped with DNA'''<br />
'''Crystal structure of E.coli formamidopyrimidine-DNA glycosylase (Fpg) covalently trapped with DNA'''<br />
==Overview==
==Overview==
-
Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that, excises oxidized purines from damaged DNA. The Schiff base intermediate, formed during this reaction between Escherichia coli Fpg and DNA was, trapped by reduction with sodium borohydride, and the structure of the, resulting covalently cross-linked complex was determined at a 2.1-A, resolution. Fpg is a bilobal protein with a wide, positively charged, DNA-binding groove. It possesses a conserved zinc finger and a helix-two, turn-helix motif that participate in DNA binding. The absolutely conserved, residues Lys-56, His-70, Asn-168, and Arg-258 form hydrogen bonds to the, phosphodiester backbone of DNA, which is sharply kinked at the lesion, site. Residues Met-73, Arg-109, and Phe-110 are inserted into the DNA, helix, filling the void created by nucleotide eversion. A deep hydrophobic, pocket in the active site is positioned to accommodate an everted base., Structural analysis of the Fpg-DNA complex reveals essential features of, damage recognition and the catalytic mechanism of Fpg.
+
Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. The Schiff base intermediate formed during this reaction between Escherichia coli Fpg and DNA was trapped by reduction with sodium borohydride, and the structure of the resulting covalently cross-linked complex was determined at a 2.1-A resolution. Fpg is a bilobal protein with a wide, positively charged DNA-binding groove. It possesses a conserved zinc finger and a helix-two turn-helix motif that participate in DNA binding. The absolutely conserved residues Lys-56, His-70, Asn-168, and Arg-258 form hydrogen bonds to the phosphodiester backbone of DNA, which is sharply kinked at the lesion site. Residues Met-73, Arg-109, and Phe-110 are inserted into the DNA helix, filling the void created by nucleotide eversion. A deep hydrophobic pocket in the active site is positioned to accommodate an everted base. Structural analysis of the Fpg-DNA complex reveals essential features of damage recognition and the catalytic mechanism of Fpg.
==About this Structure==
==About this Structure==
-
1K82 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1K82 OCA].
+
1K82 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1K82 OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Fernandes, A.S.]]
+
[[Category: Fernandes, A S.]]
-
[[Category: Gerchman, S.E.]]
+
[[Category: Gerchman, S E.]]
[[Category: Gilboa, R.]]
[[Category: Gilboa, R.]]
[[Category: Golan, G.]]
[[Category: Golan, G.]]
-
[[Category: Grollman, A.P.]]
+
[[Category: Grollman, A P.]]
-
[[Category: Kycia, J.H.]]
+
[[Category: Kycia, J H.]]
[[Category: Matz, E.]]
[[Category: Matz, E.]]
[[Category: Shoham, G.]]
[[Category: Shoham, G.]]
-
[[Category: Zharkov, D.O.]]
+
[[Category: Zharkov, D O.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: beta sandwich]]
[[Category: beta sandwich]]
Line 30: Line 30:
[[Category: zinc finger]]
[[Category: zinc finger]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:56:11 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:06 2008''

Revision as of 11:31, 21 February 2008


1k82, resolution 2.10Å

Drag the structure with the mouse to rotate

Crystal structure of E.coli formamidopyrimidine-DNA glycosylase (Fpg) covalently trapped with DNA

Overview

Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. The Schiff base intermediate formed during this reaction between Escherichia coli Fpg and DNA was trapped by reduction with sodium borohydride, and the structure of the resulting covalently cross-linked complex was determined at a 2.1-A resolution. Fpg is a bilobal protein with a wide, positively charged DNA-binding groove. It possesses a conserved zinc finger and a helix-two turn-helix motif that participate in DNA binding. The absolutely conserved residues Lys-56, His-70, Asn-168, and Arg-258 form hydrogen bonds to the phosphodiester backbone of DNA, which is sharply kinked at the lesion site. Residues Met-73, Arg-109, and Phe-110 are inserted into the DNA helix, filling the void created by nucleotide eversion. A deep hydrophobic pocket in the active site is positioned to accommodate an everted base. Structural analysis of the Fpg-DNA complex reveals essential features of damage recognition and the catalytic mechanism of Fpg.

About this Structure

1K82 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as DNA-formamidopyrimidine glycosylase, with EC number 3.2.2.23 Full crystallographic information is available from OCA.

Reference

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA., Gilboa R, Zharkov DO, Golan G, Fernandes AS, Gerchman SE, Matz E, Kycia JH, Grollman AP, Shoham G, J Biol Chem. 2002 May 31;277(22):19811-6. Epub 2002 Mar 23. PMID:11912217

Page seeded by OCA on Thu Feb 21 13:31:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools