1k98
From Proteopedia
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| , resolution 3.75Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Methionine synthase, with EC number 2.1.1.13 | ||||||
| Related: | 1msk, 1bmd, 1k7y
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
AdoMet complex of MetH C-terminal fragment
Overview
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 A structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 A and rotates by 63 degrees, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations.
About this Structure
1K98 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Domain alternation switches B(12)-dependent methionine synthase to the activation conformation., Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML, Nat Struct Biol. 2002 Jan;9(1):53-6. PMID:11731805
Page seeded by OCA on Sun Mar 30 21:45:13 2008
