1hd7: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1hd7.jpg|left|200px]]
{{Seed}}
[[Image:1hd7.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hd7|  PDB=1hd7  |  SCENE=  }}  
{{STRUCTURE_1hd7|  PDB=1hd7  |  SCENE=  }}  


'''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===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_11286553}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11286553 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11286553}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hap1]]
[[Category: Hap1]]
[[Category: Ref-1]]
[[Category: Ref-1]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:43:18 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:01:03 2008''

Revision as of 05:01, 1 July 2008

File:1hd7.png

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

Template:ABSTRACT PUBMED 11286553

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 Tue Jul 1 08:01:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1hd7&oldid=606590"