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Article

Crystal structure and solution characterization of the activation domain of human methionine synthase.

The FEBS journal - 1 Feb 2007

Wolthers Kirsten R, Toogood Helen S, Jowitt Thomas A, Marshall Ker R, Leys David, Scrutton Nigel S

Abstract excerpt

Human methionine synthase (hMS) is a multidomain cobalamin-dependent enzyme that catalyses the conversion of homocysteine to methionine by methyl group transfer. We report here the 1.6 A crystal structure of the C-terminal activation domain of hMS. The structure is C-shaped with the core comprisi...

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Source

Identifiers

PMID: 17288554
DOI: 10.1111/j.1742-4658.2006.05618.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17288554-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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