3bdp: Difference between revisions

Revision as of 06:38, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bdp.png

Template:STRUCTURE 3bdp

DNA POLYMERASE I/DNA COMPLEXDNA POLYMERASE I/DNA COMPLEX

Template:ABSTRACT PUBMED 9440698

About this StructureAbout this Structure

3BDP is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal., Kiefer JR, Mao C, Braman JC, Beese LS, Nature. 1998 Jan 15;391(6664):304-7. PMID:9440698

Page seeded by OCA on Mon Jul 28 06:38:43 2008

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OCA

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 {{STRUCTURE_3bdp|  PDB=3bdp  |  SCENE=  }}
-'''DNA POLYMERASE I/DNA COMPLEX'''
+===DNA POLYMERASE I/DNA COMPLEX===
-==Overview==
+<!--
-DNA polymerases copy DNA templates with remarkably high fidelity, checking for correct base-pair formation both at nucleotide insertion and at subsequent DNA extension steps. Despite extensive biochemical, genetic and structural studies, the mechanism by which nucleotides are correctly incorporated is not known. Here we present high-resolution crystal structures of a thermostable bacterial (Bacillus stearothermophilus) DNA polymerase I large fragments with DNA primer templates bound productively at the polymerase active site. The active site retains catalytic activity, allowing direct observation of the products of several rounds of nucleotide incorporation. The polymerase also retains its ability to discriminate between correct and incorrectly paired nucleotides in the crystal. Comparison of the structures of successively translocated complexes allows the structural features for the sequence-independent molecular recognition of correctly formed base pairs to be deduced unambiguously. These include extensive interactions with the first four to five base pairs in the minor groove, location of the terminal base pair in a pocket of excellent steric complementarity favouring correct base-pair formation, and a conformational switch from B-form to underwound A-form DNA at the polymerase active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_9440698}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9440698 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9440698}}
 ==About this Structure==
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 [[Category: Bacillus stearothermophilus dna polymerase]]
 [[Category: Bf thermophilus polymerase]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:38:43 2008''