2riq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2riq.jpg|left|200px]] | [[Image:2riq.jpg|left|200px]] | ||
'''Crystal Structure of the Third Zinc-binding domain of human PARP-1''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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] | |||
|GENE= PARP1, ADPRT, PPOL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal Structure of the Third Zinc-binding domain of human PARP-1''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2RIQ is a [ | 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== | ||
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:// | 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]] | ||
| Line 37: | 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 Thu Mar 20 18:36:31 2008'' | ||
Revision as of 16:36, 20 March 2008
| |||||||||||||
| 2riq, resolution 1.70Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1, AC2, AC3, AC4 and AC5 | ||||||||||||
| Ligands: | ZN, EOH and GOL | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 18:36:31 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Homo sapiens
- NAD(+) ADP-ribosyltransferase
- Single protein
- Langelier, M F.
- Pascal, J M.
- Servent, K M.
- EOH
- GOL
- ZN
- 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
