Talk:Methionine synthase
From Proteopedia
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This has the N-terminal half of the protein, including the homocysteine binding domain.<ref>PMID:18296644</ref> | This has the N-terminal half of the protein, including the homocysteine binding domain.<ref>PMID:18296644</ref> | ||
| - | Here is some information on the reactivation mechanism.<ref>DOI: | + | Here is some information on the reactivation mechanism.<ref>DOI:0.1073/pnas.0906132106</ref> |
Some methionine synthases don't make use of the folate cycle.<ref>DOI:10.1371/journal. | Some methionine synthases don't make use of the folate cycle.<ref>DOI:10.1371/journal. | ||
Revision as of 21:12, 4 April 2022
There is a related protein where the entire structure was solved:
If you don't want to watch the entire thing, skip ahead to 31:20
The paper is here.[1]
This has the N-terminal half of the protein, including the homocysteine binding domain.[2]
Here is some information on the reactivation mechanism.[3]
Some methionine synthases don't make use of the folate cycle.[4]
Predicted entire structure
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- ↑ Kung Y, Ando N, Doukov TI, Blasiak LC, Bender G, Seravalli J, Ragsdale SW, Drennan CL. Visualizing molecular juggling within a B(12)-dependent methyltransferase complex. Nature. 2012 Mar 14. doi: 10.1038/nature10916. PMID:22419154 doi:10.1038/nature10916
- ↑ Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML. Metal active site elasticity linked to activation of homocysteine in methionine synthases. Proc Natl Acad Sci U S A. 2008 Mar 4;105(9):3286-91. Epub 2008 Feb 22. PMID:18296644
- ↑ doi: https://dx.doi.org/0.1073/pnas.0906132106
- ↑ doi: https://dx.doi.org/10.1371/journal.pgen.100934
