1k98: Difference between revisions
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|PDB= 1k98 |SIZE=350|CAPTION= <scene name='initialview01'>1k98</scene>, resolution 3.75Å | |PDB= 1k98 |SIZE=350|CAPTION= <scene name='initialview01'>1k98</scene>, resolution 3.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1msk|1msk]], [[1bmd|1bmd]], [[1k7y|1k7y]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k98 OCA], [http://www.ebi.ac.uk/pdbsum/1k98 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k98 RCSB]</span> | |||
}} | }} | ||
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[[Category: Matthews, R G.]] | [[Category: Matthews, R G.]] | ||
[[Category: Pattridge, K A.]] | [[Category: Pattridge, K A.]] | ||
[[Category: adomet binding]] | [[Category: adomet binding]] | ||
[[Category: domain interaction]] | [[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 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:13 2008'' | ||
Revision as of 18:45, 30 March 2008
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| 1k98, resolution 3.75Å | |||||||||||||
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| Ligands: | B12, SO4 | ||||||||||||
| 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
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