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Structure paper

TitleKinetic, thermodynamic, and structural insight into the mechanism of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis.
Journal, issue, pagesJ. Mol. Biol., Vol. 404, Page 202-219, Year 2010
Publish dateJun 3, 2010 (structure data deposition date)
AuthorsWubben, T.J. / Mesecar, A.D.
External linksJ. Mol. Biol. / PubMed:20851704
MethodsX-ray diffraction
Resolution1.58 - 2.68 Å
Structure data

PDB-3nba:
Phosphopantetheine Adenylyltranferase from Mycobacterium tuberculosis in complex with adenosine-5'-[(alpha,beta)-methyleno]triphosphate (AMPCPP)
Method: X-RAY DIFFRACTION / Resolution: 2.68 Å

PDB-3nbk:
Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis in complex with 4'-phosphopantetheine
Method: X-RAY DIFFRACTION / Resolution: 1.58 Å

Chemicals

ChemComp-APC:
DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER / AMP-CPP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PNS:
4'-PHOSPHOPANTETHEINE

ChemComp-NI:
NICKEL (II) ION

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSFERASE / PPAT / AMPCPP / phosphopantetheine adenylyltransferase / tuberculosis / PhP / pantetheine

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