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2riq
From Proteopedia
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|PDB= 2riq |SIZE=350|CAPTION= <scene name='initialview01'>2riq</scene>, resolution 1.70Å | |PDB= 2riq |SIZE=350|CAPTION= <scene name='initialview01'>2riq</scene>, resolution 1.70Å | ||
|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> | |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> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= PARP1, ADPRT, PPOL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PARP1, ADPRT, PPOL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2riq OCA], [http://www.ebi.ac.uk/pdbsum/2riq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2riq RCSB]</span> | ||
}} | }} | ||
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[[Category: Pascal, J M.]] | [[Category: Pascal, J M.]] | ||
[[Category: Servent, K M.]] | [[Category: Servent, K M.]] | ||
| - | [[Category: EOH]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: ZN]] | ||
[[Category: adp-ribosylation]] | [[Category: adp-ribosylation]] | ||
[[Category: dna damage]] | [[Category: dna damage]] | ||
| Line 46: | Line 46: | ||
[[Category: zn-binding domain]] | [[Category: zn-binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:00:56 2008'' |
Revision as of 02:00, 31 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , and | ||||||
| Ligands: | , , | ||||||
| Gene: | PARP1, ADPRT, PPOL (Homo sapiens) | ||||||
| Activity: | NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 05:00:56 2008
Categories: Homo sapiens | NAD(+) ADP-ribosyltransferase | Single protein | Langelier, M F. | Pascal, J M. | Servent, K M. | Adp-ribosylation | Dna damage | Dna repair | Dna-binding | Glycosyltransferase | Metal-binding | Nad | Nucleus | Phosphorylation | Polymorphism | Transferase | Zinc | Zinc-finger | Zn finger | Zn ribbon | Zn-binding domain
