Methionine adenosyltransferase complexed with both substrates ATP and methionine

Crystal Structures of Methionine Adenosyltransferase Complexed with Substrates and Products Reveal the Methionine-ATP Recognition and Give Insights Into the Catalytic Mechanism

The Crystal Structure of Tetrameric Methionine Adenosyltransferase Fom Rat Liver Reveals the Methionine Binding Site

METHIONINE ADENOSYLTRANSFERASE, ADOMET SYNTHETASE, MAT-I

MNGPVDGLCDHSLSEEGAFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMIDY
QRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIVLAHK
LNTRMADLRRSGVLPWLRPDSKTQVTVQYVQDNGAVIPVRVHTIVISVQHNEDITLEAMREALKEQVIKAVVPAKYLDED
TIYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVS
YAIGVAEPLSISIFTYGTSKKTERELLEVVNKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPKKLVF

16% PEG 10000, 10MM L-METHIONINE, 100MM HEPES PH=7.5 (SOAKING IN 30 MM ATP SOLUTION), pH 7.50

METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH A L-METHIONINE ANALOGOUS

METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH ADP AND A L-METHIONINE ANALOGOUS

METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH ATP AND A L-METHIONINE ANALOGOUS

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

CATALYSES THE REACTION BETWEEN ATP AND L-METHIONINE, RESULTING IN THE FORMATION OF S-ADENOSYLMETHIONINE
THE SWISS-PROT ACCESSION FOR THIS ENTRY P13444 HAS A RESIDUE ASN AT POSITION 345. THE DEPOSITORS INDICATE THAT THIS IS A POSSIBLE ERROR IN THE SWISS-PROT DATABASE ENTRY FOR THIS PROTEIN, AND THAT RESIDUE 345 ASN DOES DOES NOT EXIST IN THE STRUCTURE WHICH IS DESCRIBED HERE. THE DBREF CONSEQUENTLY MAPS TO THE SWISS-PROT ENTRY IN TWO PARTS AS SHOWN BELOW.

TRANSFERASE, ADENOSYLTRANSFERASE, ATP BINDING, METHIONINE BINDING, ONE-CARBON METABOLISM, MAGNESIUM, POTASSIUM, METAL-BINDING, MULTIGENE FAMILY, ATP-BINDING