(Q27642622)

2

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Jimin Wang

3

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Alan M Weiner

4

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Thomas A Steitz

DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history

5

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publication date

November 2003

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published in

Molecular Cell

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volume

12

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issue

5

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page(s)

1165-72

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cites work

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Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization

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Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP

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Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase

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Ribosomes and translation

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DNA polymerase beta belongs to an ancient nucleotidyltransferase superfamily

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Touring protein fold space with Dali/FSSP

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Polymerase structures and function: variations on a theme?

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Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: A scrunching-shuttling model of CCA specificity

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Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP

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Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP

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Refinement of macromolecular structures by the maximum-likelihood method

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The structural basis of ribosome activity in peptide bond synthesis

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Processing of X-ray diffraction data collected in oscillation mode

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Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP

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Functional overlap of tRNA nucleotidyltransferase, poly(A) polymerase I, and polynucleotide phosphorylase

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Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution

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Poly(C) synthesis by class I and class II CCA-adding enzymes

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CCA addition by tRNA nucleotidyltransferase: polymerization without translocation?

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A mechanism for all polymerases

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Automated MAD and MIR structure solution

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RNA recognition by RNP proteins during RNA processing

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The CCA-adding enzyme has a single active site

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Threonyl-tRNA synthetase from Thermus thermophilus: purification and some structural and kinetic properties.

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