Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair (Q27628392)

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2 November 2019

title

Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair (English)

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2 November 2019

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M M Skinner

1

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2 November 2019

J M Puvathingal

series ordinal

2

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2 November 2019

R L Walter

series ordinal

3

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2 November 2019

A M Friedman

series ordinal

4

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2 November 2019

publication date

1 November 2000

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2 November 2019

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2 November 2019

volume

8

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2 November 2019

issue

11

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2 November 2019

page(s)

1189-1201

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Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins

2 November 2019

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Isolation and characterization of 101-succinimide lysozyme that possesses the cyclic imide at Asp101-Gly102

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Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose

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Identification of an isoaspartyl linkage formed upon deamidation of bovine calbindin D9k and structural characterization by 2D 1H NMR.

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Deamidation in proteins: the crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67

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Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

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Crystal structure of catechol O-methyltransferase

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Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes

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7 January 2021

The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing

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7 January 2021

Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine

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Kinetic properties of bovine brain protein L-isoaspartyl methyltransferase determined using a synthetic isoaspartyl peptide substrate

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Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment

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Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes

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Identifiers

DOI

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2 November 2019

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