Structural basis for proofreading during replication of the Escherichia coli chromosome

Samir Hamdan; Paul D. Carr; Susan E. Brown; David L. Ollis; Nicholas E. Dixon

doi:10.1016/S0969-2126(02)00738-4

Structural basis for proofreading during replication of the Escherichia coli chromosome

Samir Hamdan, Paul D. Carr, Susan E. Brown, David L. Ollis, Nicholas E. Dixon^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

128 Citations (Scopus)

Abstract

The ε subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3′-5′ exonuclease. Structures of its catalytic N-terminal domain (ε186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 Å, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5′-monophosphate. The protein structure is built around a core five-stranded β sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for ε and to produce a plausible model of the complex of ε186 with DNA.

Original language	English
Pages (from-to)	535-546
Number of pages	12
Journal	Structure
Volume	10
Issue number	4
DOIs	https://doi.org/10.1016/S0969-2126(02)00738-4
Publication status	Published - 2002

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title = "Structural basis for proofreading during replication of the Escherichia coli chromosome",

abstract = "The ε subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3′-5′ exonuclease. Structures of its catalytic N-terminal domain (ε186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 {\AA}, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5′-monophosphate. The protein structure is built around a core five-stranded β sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for ε and to produce a plausible model of the complex of ε186 with DNA.",

keywords = "Binuclear metallohydrolase, DNA polymerase III, DNA replication, DnaQ, Exonuclease (3′-5′), Manganese metalloenzyme, X-ray crystallography",

author = "Samir Hamdan and Carr, {Paul D.} and Brown, {Susan E.} and Ollis, {David L.} and Dixon, {Nicholas E.}",

year = "2002",

doi = "10.1016/S0969-2126(02)00738-4",

language = "English",

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pages = "535--546",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "4",

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TY - JOUR

T1 - Structural basis for proofreading during replication of the Escherichia coli chromosome

AU - Hamdan, Samir

AU - Carr, Paul D.

AU - Brown, Susan E.

AU - Ollis, David L.

AU - Dixon, Nicholas E.

PY - 2002

Y1 - 2002

N2 - The ε subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3′-5′ exonuclease. Structures of its catalytic N-terminal domain (ε186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 Å, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5′-monophosphate. The protein structure is built around a core five-stranded β sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for ε and to produce a plausible model of the complex of ε186 with DNA.

AB - The ε subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3′-5′ exonuclease. Structures of its catalytic N-terminal domain (ε186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 Å, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5′-monophosphate. The protein structure is built around a core five-stranded β sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for ε and to produce a plausible model of the complex of ε186 with DNA.

KW - Binuclear metallohydrolase

KW - DNA polymerase III

KW - DNA replication

KW - DnaQ

KW - Exonuclease (3′-5′)

KW - Manganese metalloenzyme

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=0036229246&partnerID=8YFLogxK

U2 - 10.1016/S0969-2126(02)00738-4

DO - 10.1016/S0969-2126(02)00738-4

M3 - Article

SN - 0969-2126

VL - 10

SP - 535

EP - 546

JO - Structure

JF - Structure

IS - 4

ER -

Structural basis for proofreading during replication of the Escherichia coli chromosome

Abstract

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