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Structure paper

TitleComplexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 66, Page 181-189, Year 2010
Publish dateSep 2, 2009 (structure data deposition date)
AuthorsBale, S. / Baba, K. / McCloskey, D.E. / Pegg, A.E. / Ealick, S.E.
External linksActa Crystallogr. ,Sect. D / PubMed:20124698
MethodsX-ray diffraction
Resolution1.9 - 2.06 Å
Structure data

PDB-3iwb:
T. maritima AdoMetDC in processed form
Method: X-RAY DIFFRACTION / Resolution: 2.06 Å

PDB-3iwc:
T. maritima AdoMetDC complex with S-Adenosylmethionine methyl ester
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3iwd:
T. maritima AdoMetDC complex with 5'-Deoxy-5'-dimethyl thioadenosine
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SMM:
S-ADENOSYLMETHIONINE METHYL ESTER

ChemComp-M2T:
5'-deoxy-5'-(dimethyl-lambda~4~-sulfanyl)adenosine

Source
  • thermotoga maritima (bacteria)
KeywordsLYASE / Autocatalytic cleavage / Decarboxylase / Polyamine biosynthesis / Pyruvate / S-adenosyl-L-methionine / Schiff base / Spermidine biosynthesis / Zymogen

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