2a1k: Difference between revisions

Revision as of 08:06, 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:2a1k.png

Template:STRUCTURE 2a1k

RB69 single-stranded DNA binding protein core domainRB69 single-stranded DNA binding protein core domain

Template:ABSTRACT PUBMED 16881051

About this StructureAbout this Structure

2A1K is a Single protein structure of sequence from Enterobacteria phage rb69. Full crystallographic information is available from OCA.

ReferenceReference

Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity., Sun S, Geng L, Shamoo Y, Proteins. 2006 Oct 1;65(1):231-8. PMID:16881051

Page seeded by OCA on Mon Jul 28 08:06:54 2008

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OCA

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-'''RB69 single-stranded DNA binding protein core domain'''
+===RB69 single-stranded DNA binding protein core domain===
-==Overview==
+<!--
-In vivo, replicative DNA polymerases are made more processive by their interactions with accessory proteins at the replication fork. Single-stranded DNA binding protein (SSB) is an essential protein that binds tightly and cooperatively to single-stranded DNA during replication to remove adventitious secondary structures and protect the exposed DNA from endogenous nucleases. Using information from high resolution structures and biochemical data, we have engineered a functional chimeric enzyme of the bacteriophage RB69 DNA polymerase and SSB with substantially increased processivity. Fusion of RB69 DNA polymerase with its cognate SSB via a short six amino acid linker increases affinity for primer-template DNA by sixfold and subsequently increases processivity by sevenfold while maintaining fidelity. The crystal structure of this fusion protein was solved by a combination of multiwavelength anomalous diffraction and molecular replacement to 3.2 A resolution and shows that RB69 SSB is positioned proximal to the N-terminal domain of RB69 DNA polymerase near the template strand channel. The structural and biochemical data suggest that SSB interactions with DNA polymerase are transient and flexible, consistent with models of a dynamic replisome during elongation.
+The line below this paragraph, {{ABSTRACT_PUBMED_16881051}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Single-stranded dna binding]]
 [[Category: Zn2+ binding subdomain]]
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