Crystal structure of apo transketolase from Chlamydomonas reinhardtii

Structural basis for the magnesium-dependent activation of transketolase from Chlamydomonas reinhardtii.

MHHHHHHHMAAQAAPAAAKAAAPSISRDEVEKCINAIRFLAIDAINKSKSGHPGMPMGCAPMGYVLWNEVMKYNPKNPDF
FNRDRFVLSAGHGSMFQYSMMHLTGYDSVPLDQIKQFRQWNSLTPGHPENFVTPGVEVTTGPLGQGICNAVGLAVAEAHL
AARFNKPDVKPIVDHYTYCILGDGCMMEGISNEACSLAGHWGLGKLIALYDDNKISIDGHTDISFTEDVAKRYEALGWHV
IHVINGNTDVDGLRAAIAQAKAVKDKPTLIKVSTLIGYGSPNKADSHDVHGAPLGPDETAATRKNLNWPYGEFEVPQDVY
DVFRGAIKRGAEEEANWHKACAEYKAKYPKEWAEFEALTSCKLPENWEAALPHFKPEDKGLATRQHSQTMINALAPALPG
LIGGSADLAPSNLTLMKISGDFQKGSYAERNLRFGVREHAMGAICNGIALHKSGLIPYCATFYIFTDYMRNAMRMSALSE
AGVVYVMTHDSIGLGEDGPTHQPIEHLASFRAMPDMLMIRPAGGNETAGAYKVAIANRKRPTTIALSRQNMPNIPNCSVE
GVAKGAYTIHDTKAGVKPDVILMGTGSELELATAAAGILEKEGKNVRVVSFPCWELFEEQSAEYKESVLPSDVTARVSVE
AATSFGWAKYIGLKGKHVGIDTFGASAPAPTLYEKFGITVNHVVEAAKATLQH

10 % w/v PEG 6K, 5 % v/v MPD and 0.1 M MES pH 6.5-7.0 or 0.1 M HEPES pH 7.0-8.0.

University of Bologna, Alma Mater Studiourum

Biological assembly was confirmed also by gel filtration

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

TRANSFERASE, Calvin-Benson cycle, thiamine pyrophosphate, Magnesium-dependent activation

AQAAPAAAKAAAPSISRDEVEKCINAIRFLAIDAINKSKSGHPGMPMGCAPMGYVLWNEVMKYNPKNPDFFNRDRFVLSA
GHGSMFQYSMMHLTGYDSVPLDQIKQFRQWNSLTPGHPENFVTPGVEVTTGPLGQGICNAVGLAVAEAHLAARFNKPDVK
PIVDHYTYCILGDGCMMEGISNEACSLAGHWGLGKLIALYDDNKISIDGHTDISFTEDVAKRYEALGWHVIHVINGNTDV
DGLRAAIAQAKAVKDKPTLIKVSTLIGYGSPNKADSHDVHGAPLGPDETAATRKNLNWPYGEFEVPQDVYDVFRGAIKRG
AEEEANWHKACAEYKAKYPKEWAEFEALTSCKLPENWEAALPHFKPEDKGLATRQHSQTMINALAPALPGLIGGSADLAP
SNLTLMKISGDFQKGSYAERNLRFGVREHAMGAICNGIALHKSGLIPYCATFYIFTDYMRNAMRMSALSEAGVVYVMTHD
SIGLGEDGPTHQPIEHLASFRAMPDMLMIRPAGGNETAGAYKVAIANRKRPTTIALSRQNMPNIPNCSVEGVAKGAYTIH
DTKAGVKPDVILMGTGSELELATAAAGILEKEGKNVRVVSFPCWELFEEQSAEYKESVLPSDVTARVSVEAATSFGWAKY
IGLKGKHVGIDTFGASAPAPTLYEKFGITVNHVVEAAKATLQH