1k98
From Proteopedia
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| - | [[Image:1k98.jpg|left|200px]] | + | [[Image:1k98.jpg|left|200px]] |
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| - | '''AdoMet complex of MetH C-terminal fragment''' | + | {{Structure |
| + | |PDB= 1k98 |SIZE=350|CAPTION= <scene name='initialview01'>1k98</scene>, resolution 3.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=B12:COBALAMIN'>B12</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methionine_synthase Methionine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.13 2.1.1.13] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''AdoMet complex of MetH C-terminal fragment''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K98 is a [ | + | 1K98 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K98 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11731805 11731805] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Methionine synthase]] | [[Category: Methionine synthase]] | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: adomet binding]] | [[Category: adomet binding]] | ||
| - | [[Category: domain | + | [[Category: domain interaction]] |
[[Category: motion of 4-helix bundle]] | [[Category: motion of 4-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:14:14 2008'' |
Revision as of 10:14, 20 March 2008
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| , resolution 3.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Methionine synthase, with EC number 2.1.1.13 | ||||||
| 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
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