1hd7

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[[Image:1hd7.jpg|left|200px]]
[[Image:1hd7.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1hd7 |SIZE=350|CAPTION= <scene name='initialview01'>1hd7</scene>, resolution 1.95&Aring;
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The line below this paragraph, containing "STRUCTURE_1hd7", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=PB1:Pb+Binding+Site'>PB1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1hd7| PDB=1hd7 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hd7 OCA], [http://www.ebi.ac.uk/pdbsum/1hd7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hd7 RCSB]</span>
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}}
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'''A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIDINIMIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM'''
'''A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIDINIMIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM'''
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==Reference==
==Reference==
Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism., Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B, J Mol Biol. 2001 Apr 6;307(4):1023-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11286553 11286553]
Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism., Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B, J Mol Biol. 2001 Apr 6;307(4):1023-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11286553 11286553]
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[[Category: DNA-(apurinic or apyrimidinic site) lyase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Segelke, B W.]]
[[Category: Segelke, B W.]]
[[Category: Wilson, D M.]]
[[Category: Wilson, D M.]]
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[[Category: ape1]]
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[[Category: Ape1]]
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[[Category: dna repair]]
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[[Category: Dna repair]]
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[[Category: endonuclease]]
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[[Category: Endonuclease]]
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[[Category: hap1]]
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[[Category: Hap1]]
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[[Category: ref-1]]
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[[Category: Ref-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:43:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:02:41 2008''
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Revision as of 15:43, 2 May 2008

Image:1hd7.jpg

Template:STRUCTURE 1hd7

A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIDINIMIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM


Overview

The major human abasic endonuclease, Ape1, is an essential DNA repair enzyme that initiates the removal of apurinic/apyrimidinic sites from DNA, excises 3' replication-blocking moieties, and modulates the DNA binding activity of several transcriptional regulators. We have determined the X-ray structure of the full-length human Ape1 enzyme in two new crystal forms, one at neutral and one at acidic pH. The new structures are generally similar to the previously determined structure of a truncated Ape1 protein, but differ in the conformation of several loop regions and in spans of residues with weak electron density. While only one active-site metal ion is present in the structure determined at low pH, the structure determined from a crystal grown at the pH optimum of Ape1 nuclease activity, pH 7.5, has two metal ions bound 5 A apart in the active site. Enzyme kinetic data indicate that at least two metal-binding sites are functionally important, since Ca(2+) exhibits complex stimulatory and inhibitory effects on the Mg(2+)-dependent catalysis of Ape1, even though Ca(2+) itself does not serve as a cofactor. In conjunction, the structural and kinetic data suggest that Ape1 catalyzes hydrolysis of the DNA backbone through a two metal ion-mediated mechanism.

About this Structure

1HD7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism., Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B, J Mol Biol. 2001 Apr 6;307(4):1023-34. PMID:11286553 Page seeded by OCA on Fri May 2 18:43:18 2008

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