1q85

Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima (Cd2+ complex, Se-Met)

spinqualitylabelsall models 1q85, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1q85 is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CD, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9WYA5_THEMA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine synthase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA