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TitleEvolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure-function constrains.
Journal, issue, pagesProtein Sci., Vol. 31, Page e4352-e4352, Year 2022
Publish dateFeb 6, 2022 (structure data deposition date)
AuthorsKleiner, D. / Shapiro Tuchman, Z. / Shmulevich, F. / Shahar, A. / Zarivach, R. / Kosloff, M. / Bershtein, S.
External linksProtein Sci. / PubMed:35762725
MethodsX-ray diffraction
Resolution1.6 - 2.82 Å
Structure data

PDB-7r2w:
Mutant S-adenosylmethionine synthetase from E.coli complexed with AMPPNP and methionine
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-7r3b:
S-adenosylmethionine synthetase from Lactobacillus plantarum complexed with AMPPNP, methionine and SAM
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PHE:
PHENYLALANINE

ChemComp-PPK:
(DIPHOSPHONO)AMINOPHOSPHONIC ACID

ChemComp-SAM:
S-ADENOSYLMETHIONINE

Source
  • escherichia coli (E. coli)
  • lactiplantibacillus plantarum (bacteria)
KeywordsTRANSFERASE / Dihedral D2 symmetry / homotetramer A4 symmetry / isologous interfaces 2 / S-adenosylmethionine synthetase

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