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Structure paper

TitleThe structural basis of chain length control in Rv1086.
Journal, issue, pagesJ. Mol. Biol., Vol. 381, Page 129-140, Year 2008
Publish dateNov 5, 2007 (structure data deposition date)
AuthorsWang, W. / Dong, C. / McNeil, M. / Kaur, D. / Mahapatra, S. / Crick, D.C. / Naismith, J.H.
External linksJ. Mol. Biol. / PubMed:18597781
MethodsX-ray diffraction
Resolution1.7 - 2.6 Å
Structure data

PDB-2vfw:
Rv1086 native
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2vg0:
Rv1086 citronellyl pyrophosphate complex
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-2vg1:
Rv1086 E,E-farnesyl diphosphate complex
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-2vg2:
Rv2361 with IPP
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-2vg3:
Rv2361 with citronellyl pyrophosphate
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2vg4:
Rv2361 native
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GPP:
GERANYL DIPHOSPHATE

ChemComp-GOL:
GLYCEROL

ChemComp-PO4:
PHOSPHATE ION

ChemComp-FPP:
FARNESYL DIPHOSPHATE

ChemComp-DPO:
DIPHOSPHATE

ChemComp-IPE:
3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE

ChemComp-CL:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSFERASE / PEPTIDOGLYCAN SYNTHESIS / CELL WALL BIOGENESIS/DEGRADATION / SECRETED / CELL SHAPE / PRENYLTRANSFERASE / CELL CYCLE / CELL DIVISION / PRENYL TRANSFERASE

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