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Structure paper

TitleQuaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes.
Journal, issue, pagesStructure, Vol. 15, Page 1555-1566, Year 2007
Publish dateJul 24, 2007 (structure data deposition date)
AuthorsSegura-Pena, D. / Lichter, J. / Trani, M. / Konrad, M. / Lavie, A. / Lutz, S.
External linksStructure / PubMed:18073106
MethodsX-ray diffraction
Resolution1.5 - 1.95 Å
Structure data

PDB-2qpo:
Thermotoga Maritima Thymidine Kinase in the apo form
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-2qq0:
Thymidine Kinase from Thermotoga Maritima in complex with thymidine + AppNHp
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2qqe:
Thymidine Kinase from Thermotoga Maritima in complex with Thymidine
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-THM:
THYMIDINE

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

ChemComp-TMP:
THYMIDINE-5'-PHOSPHATE

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • thermotoga maritima (bacteria)
KeywordsTRANSFERASE / Apo-form / ATP-binding / Cytoplasm / DNA synthesis / Kinase / Nucleotide-binding / Thymidine Kinase / TmTK / AppNHp / open-conformation / TmTK in complex with thymidine / Close conformation

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