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Structure paper

TitleStructural studies on M. tuberculosis argininosuccinate lyase and its liganded complex: Insights into catalytic mechanism.
Journal, issue, pagesIUBMB Life, Vol. 71, Page 643-652, Year 2019
Publish dateSep 14, 2018 (structure data deposition date)
AuthorsPaul, A. / Mishra, A. / Surolia, A. / Vijayan, M.
External linksIUBMB Life / PubMed:30615268
MethodsX-ray diffraction
Resolution2.2 - 2.7 Å
Structure data

PDB-6iem:
Argininosuccinate lyase from Mycobacterium tuberculosis
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-6ien:
Substrate/product bound Argininosuccinate lyase from Mycobacterium tuberculosis
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-P3G:
3,6,9,12,15-PENTAOXAHEPTADECANE

ChemComp-2PE:
NONAETHYLENE GLYCOL / precipitant*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

ChemComp-AS1:
ARGININOSUCCINATE

ChemComp-FUM:
FUMARIC ACID

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-ARG:
ARGININE

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsLYASE / arginine biosynthesis / mycobacterium tuberculosis / tetramer / aspartase/fumarase / concerted movement

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