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1e9n
From Proteopedia
(New page: 200px<br /> <applet load="1e9n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e9n, resolution 2.2Å" /> '''A SECOND DIVALENT ME...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1E9N 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 PB as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E9N OCA]]. | + | 1E9N 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 PB as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Sites: PB1, PB2, PB3 and PB4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E9N OCA]]. |
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11286553 11286553] | ||
| + | [[Category: DNA-(apurinic or apyrimidinic site) lyase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ref-1]] | [[Category: ref-1]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:50:52 2007'' |
Revision as of 09:46, 30 October 2007
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A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIMIDINIC 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 ... [(full description)]
About this Structure
1E9N is a [Single protein] structure of sequence from [Homo sapiens] with PB as [ligand]. Active as [DNA-(apurinic or apyrimidinic site) lyase], with EC number [4.2.99.18]. Structure known Active Sites: PB1, PB2, PB3 and PB4. 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 Tue Oct 30 11:50:52 2007
