1q7m: Difference between revisions
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|SITE= | |SITE= | ||
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|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=[[1q7q|1Q7Q]], [[1q7z|1Q7Z]], [[1q85|1Q85]], [[1q8a|1Q8A]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7m OCA], [http://www.ebi.ac.uk/pdbsum/1q7m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q7m RCSB]</span> | |||
}} | }} | ||
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[[Category: vitamin b12]] | [[Category: vitamin b12]] | ||
''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 23:09:57 2008'' | ||
Revision as of 23:09, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Methionine synthase, with EC number 2.1.1.13 | ||||||
| Related: | 1Q7Q, 1Q7Z, 1Q85, 1Q8A
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cobalamin-dependent methionine synthase (MetH) from Thermotoga maritima (Oxidized, Monoclinic)
OverviewOverview
B(12)-dependent methionine synthase (MetH) is a large modular enzyme that utilizes the cobalamin cofactor as a methyl donor or acceptor in three separate reactions. Each methyl transfer occurs at a different substrate-binding domain and requires a different arrangement of modules. In the catalytic cycle, the cobalamin-binding domain carries methylcobalamin to the homocysteine (Hcy) domain to form methionine and returns cob(I)alamin to the folate (Fol) domain for remethylation by methyltetrahydrofolate (CH(3)-H(4)folate). Here, we describe crystal structures of a fragment of MetH from Thermotoga maritima comprising the domains that bind Hcy and CH(3)-H(4)folate. These substrate-binding domains are (beta alpha)(8) barrels packed tightly against one another with their barrel axes perpendicular. The properties of the domain interface suggest that the two barrels remain associated during catalysis. The Hcy and CH(3)-H(4)folate substrates are bound at the C termini of their respective barrels in orientations that position them for reaction with cobalamin, but the two active sites are separated by approximately 50 A. To complete the catalytic cycle, the cobalamin-binding domain must travel back and forth between these distant active sites.
About this StructureAbout this Structure
1Q7M is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase., Evans JC, Huddler DP, Hilgers MT, Romanchuk G, Matthews RG, Ludwig ML, Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3729-36. Epub 2004 Jan 29. PMID:14752199
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