This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2bpg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bpg.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2bpg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bpg| PDB=2bpg | SCENE= }}
{{STRUCTURE_2bpg| PDB=2bpg | SCENE= }}
-
'''STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP'''
+
===STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP===
-
==Overview==
+
<!--
-
Two ternary complexes of rat DNA polymerase beta (pol beta), a DNA template-primer, and dideoxycytidine triphosphate (ddCTP) have been determined at 2.9 A and 3.6 A resolution, respectively. ddCTP is the triphosphate of dideoxycytidine (ddC), a nucleoside analog that targets the reverse transcriptase of human immunodeficiency virus (HIV) and is at present used to treat AIDS. Although crystals of the two complexes belong to different space groups, the structures are similar, suggesting that the polymerase-DNA-ddCTP interactions are not affected by crystal packing forces. In the pol beta active site, the attacking 3'-OH of the elongating primer, the ddCTP phosphates, and two Mg2+ ions are all clustered around Asp190, Asp192, and Asp256. Two of these residues, Asp190 and Asp256, are present in the amino acid sequences of all polymerases so far studied and are also spatially similar in the four polymerases--the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, T7 RNA polymerase, and rat DNA pol beta--whose crystal structures are now known. A two-metal ion mechanism is described for the nucleotidyl transfer reaction and may apply to all polymerases. In the ternary complex structures analyzed, pol beta binds to the DNA template-primer in a different manner from that recently proposed for other polymerase-DNA models.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7516580}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7516580 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7516580}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Wilson, S H.]]
[[Category: Wilson, S H.]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:36:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:20:00 2008''

Revision as of 01:20, 28 July 2008

Image:2bpg.png

Template:STRUCTURE 2bpg

STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP

Template:ABSTRACT PUBMED 7516580

About this Structure

2BPG is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP., Pelletier H, Sawaya MR, Kumar A, Wilson SH, Kraut J, Science. 1994 Jun 24;264(5167):1891-903. PMID:7516580

Page seeded by OCA on Mon Jul 28 04:20:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bpg"
Personal tools