1s75

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[[Image:1s75.gif|left|200px]]
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{{STRUCTURE_1s75| PDB=1s75 | SCENE= }}
{{STRUCTURE_1s75| PDB=1s75 | SCENE= }}
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'''SOLUTION STRUCTURE OF A DNA DUPLEX CONTAINING AN ALPHA-ANOMERIC ADENOSINE: INSIGHTS INTO SUBSTRATE RECOGNITION BY ENDONUCLEASE IV'''
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===SOLUTION STRUCTURE OF A DNA DUPLEX CONTAINING AN ALPHA-ANOMERIC ADENOSINE: INSIGHTS INTO SUBSTRATE RECOGNITION BY ENDONUCLEASE IV===
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==Overview==
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The cytotoxic alpha anomer of adenosine, generated in situ by radicals, must be recognized and repaired to maintain genomic stability. Endonuclease IV (Endo IV), a member of the base excision repair (BER) enzyme family, in addition to acting on abasic sites, has the auxiliary function of removing this mutagenic nucleotide in Escherichia coli. We have employed enzymatic, thermodynamic, and structural studies on DNA duplexes containing a central alpha-anomeric adenosine residue to characterize the role of DNA structure on recognition and catalysis by Endo IV. The enzyme recognizes and cleaves our alphaA-containing DNA duplexes at the site of the modification. The NMR solution structure of the DNA decamer duplex establishes that the single alpha-anomeric adenosine residue is intrahelical and stacks in a reverse Watson-Crick fashion consistent with the slight decrease in thermostability. However, the presence of this lesion confers significant changes to the global duplex conformation, resulting from a kink of the helical axis into the major groove and an opening of the minor groove emanating from the alpha-anomeric site. Interestingly, the conformation of the flanking base-paired segments is not greatly altered from a B-type conformation. The global structural changes caused by this lesion place the DNA along the conformational path leading to the DNA structure observed in the complex. Thus, it appears that the alpha-anomeric lesion facilitates recognition by Endo IV.
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The line below this paragraph, {{ABSTRACT_PUBMED_15050824}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15050824 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15050824}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S75 OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S75 OCA].
==Reference==
==Reference==
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[[Category: Pon, R T.]]
[[Category: Pon, R T.]]
[[Category: Dna double helix with enlarged miner groove and helical kink]]
[[Category: Dna double helix with enlarged miner groove and helical kink]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:22:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:35:32 2008''

Revision as of 16:35, 27 July 2008

Template:STRUCTURE 1s75

SOLUTION STRUCTURE OF A DNA DUPLEX CONTAINING AN ALPHA-ANOMERIC ADENOSINE: INSIGHTS INTO SUBSTRATE RECOGNITION BY ENDONUCLEASE IV

Template:ABSTRACT PUBMED 15050824

About this Structure

Full experimental information is available from OCA.

Reference

Solution structure of a DNA duplex containing an alpha-anomeric adenosine: insights into substrate recognition by endonuclease IV., Aramini JM, Cleaver SH, Pon RT, Cunningham RP, Germann MW, J Mol Biol. 2004 Apr 16;338(1):77-91. PMID:15050824

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