2riq

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[[Image:2riq.jpg|left|200px]]<br /><applet load="2riq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2riq.jpg|left|200px]]
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caption="2riq, resolution 1.70&Aring;" />
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'''Crystal Structure of the Third Zinc-binding domain of human PARP-1'''<br />
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{{Structure
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|PDB= 2riq |SIZE=350|CAPTION= <scene name='initialview01'>2riq</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+1'>AC1</scene>, <scene name='pdbsite=AC2:Eoh+Binding+Site+For+Residue+A+2'>AC2</scene>, <scene name='pdbsite=AC3:Gol+Binding+Site+For+Residue+A+3'>AC3</scene>, <scene name='pdbsite=AC4:Gol+Binding+Site+For+Residue+A+4'>AC4</scene> and <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+A+5'>AC5</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30]
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|GENE= PARP1, ADPRT, PPOL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of the Third Zinc-binding domain of human PARP-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2RIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=EOH:'>EOH</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+1'>AC1</scene>, <scene name='pdbsite=AC2:Eoh+Binding+Site+For+Residue+A+2'>AC2</scene>, <scene name='pdbsite=AC3:Gol+Binding+Site+For+Residue+A+3'>AC3</scene>, <scene name='pdbsite=AC4:Gol+Binding+Site+For+Residue+A+4'>AC4</scene> and <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+A+5'>AC5</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIQ OCA].
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2RIQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIQ OCA].
==Reference==
==Reference==
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A Third Zinc-binding Domain of Human Poly(ADP-ribose) Polymerase-1 Coordinates DNA-dependent Enzyme Activation., Langelier MF, Servent KM, Rogers EE, Pascal JM, J Biol Chem. 2008 Feb 15;283(7):4105-14. Epub 2007 Nov 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18055453 18055453]
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A Third Zinc-binding Domain of Human Poly(ADP-ribose) Polymerase-1 Coordinates DNA-dependent Enzyme Activation., Langelier MF, Servent KM, Rogers EE, Pascal JM, J Biol Chem. 2008 Feb 15;283(7):4105-14. Epub 2007 Nov 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18055453 18055453]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: NAD(+) ADP-ribosyltransferase]]
[[Category: NAD(+) ADP-ribosyltransferase]]
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[[Category: zn-binding domain]]
[[Category: zn-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 27 07:48:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:36:31 2008''

Revision as of 16:36, 20 March 2008

Image:2riq.jpg


PDB ID 2riq

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites: , , , and
Ligands: , and
Gene: PARP1, ADPRT, PPOL (Homo sapiens)
Activity: NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Third Zinc-binding domain of human PARP-1


Overview

Poly(ADP-ribose) polymerase-1 (PARP-1) is a chromatin-associated enzyme with multiple cellular functions, including DNA repair, transcriptional regulation, and cell signaling. PARP-1 has a modular architecture with six independent domains comprising the 113-kDa polypeptide. Two zinc finger domains at the N terminus of PARP-1 bind to DNA and thereby activate the catalytic domain situated at the C terminus of the enzyme. The tight coupling of DNA binding and catalytic activities is critical to the cellular regulation of PARP-1 function; however, the mechanism for coordinating these activities remains an unsolved problem. Here, we demonstrate using spectroscopic and crystallographic analysis that human PARP-1 has a third zinc-binding domain. Biochemical mutagenesis and deletion analysis indicate that this region mediates interdomain contacts important for DNA-dependent enzyme activation. The crystal structure of the third zinc-binding domain reveals a zinc ribbon fold and suggests conserved residues that could form interdomain contacts. The new zinc-binding domain self-associates in the crystal lattice to form a homodimer with a head-totail arrangement. The structure of the homodimer provides a scaffold for assembling the activated state of PARP-1 and suggests a mechanism for coupling the DNA binding and catalytic functions of PARP-1.

About this Structure

2RIQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A Third Zinc-binding Domain of Human Poly(ADP-ribose) Polymerase-1 Coordinates DNA-dependent Enzyme Activation., Langelier MF, Servent KM, Rogers EE, Pascal JM, J Biol Chem. 2008 Feb 15;283(7):4105-14. Epub 2007 Nov 30. PMID:18055453

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