1k7y
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1k7y.jpg|left|200px]] | [[Image:1k7y.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1k7y", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1k7y| PDB=1k7y | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''E. coli MetH C-terminal fragment (649-1227)''' | '''E. coli MetH C-terminal fragment (649-1227)''' | ||
| Line 32: | Line 29: | ||
[[Category: Matthews, R G.]] | [[Category: Matthews, R G.]] | ||
[[Category: Pattridge, K A.]] | [[Category: Pattridge, K A.]] | ||
| - | [[Category: | + | [[Category: Domain interaction]] |
| - | [[Category: | + | [[Category: Motion of 4-helix bundle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:24:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:24, 2 May 2008
E. coli MetH C-terminal fragment (649-1227)
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
1K7Y 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 Fri May 2 22:24:54 2008
