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1k98

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{{STRUCTURE_1k98| PDB=1k98 | SCENE= }}
{{STRUCTURE_1k98| PDB=1k98 | SCENE= }}
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'''AdoMet complex of MetH C-terminal fragment'''
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===AdoMet complex of MetH C-terminal fragment===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11731805 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11731805}}
==About this Structure==
==About this Structure==
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[[Category: Domain interaction]]
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[[Category: Motion of 4-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:27:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:58:52 2008''

Revision as of 06:58, 2 July 2008

Image:1k98.png

Template:STRUCTURE 1k98

AdoMet complex of MetH C-terminal fragment

Template:ABSTRACT PUBMED 11731805

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 Wed Jul 2 09:58:52 2008

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