We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1huo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1huo.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1huo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1huo| PDB=1huo | SCENE= }}
{{STRUCTURE_1huo| PDB=1huo | SCENE= }}
-
'''CRYSTAL STRUCTURE OF DNA POLYMERASE BETA COMPLEXED WITH DNA AND CR-TMPPCP'''
+
===CRYSTAL STRUCTURE OF DNA POLYMERASE BETA COMPLEXED WITH DNA AND CR-TMPPCP===
-
==Overview==
+
<!--
-
The catalytic reaction mediated by DNA polymerases is known to require two Mg(II) ions, one associated with dNTP binding and the other involved in metal ion catalysis of the chemical step. Here we report a functional intermediate structure of a DNA polymerase with only one metal ion bound, the DNA polymerase beta-DNA template-primer-chromium(III).2'-deoxythymidine 5'-beta,gamma-methylenetriphosphate [Cr(III).dTMPPCP] complex, at 2.6 A resolution. The complex is distinct from the structures of other polymerase-DNA-ddNTP complexes in that the 3'-terminus of the primer has a free hydroxyl group. Hence, this structure represents a fully functional intermediate state. Support for this contention is provided by the observation of turnover in biochemical assays of crystallized protein as well as from the determination that soaking Pol beta crystals with Mn(II) ions leads to formation of the product complex, Pol beta-DNA-Cr(III).PCP, whose structure is also reported. An important feature of both structures is that the fingers subdomain is closed, similar to structures of other ternary complexes in which both metal ion sites are occupied. These results suggest that closing of the fingers subdomain is induced specifically by binding of the metal-dNTP complex prior to binding of the catalytic Mg(2+) ion. This has led us to reevaluate our previous evidence regarding the existence of a rate-limiting conformational change in Pol beta's reaction pathway. The results of stopped-flow studies suggest that there is no detectable rate-limiting conformational change step.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11330999}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11330999 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11330999}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Zhong, X.]]
[[Category: Zhong, X.]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:14:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:43:42 2008''

Revision as of 05:43, 1 July 2008

Image:1huo.png

Template:STRUCTURE 1huo

CRYSTAL STRUCTURE OF DNA POLYMERASE BETA COMPLEXED WITH DNA AND CR-TMPPCP

Template:ABSTRACT PUBMED 11330999

About this Structure

1HUO is a Single protein structure of sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 1cf6. Full crystallographic information is available from OCA.

Reference

Insight into the catalytic mechanism of DNA polymerase beta: structures of intermediate complexes., Arndt JW, Gong W, Zhong X, Showalter AK, Liu J, Dunlap CA, Lin Z, Paxson C, Tsai MD, Chan MK, Biochemistry. 2001 May 8;40(18):5368-75. PMID:11330999

Page seeded by OCA on Tue Jul 1 08:43:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1huo"
Personal tools