Structure of a Circular Permutation on Lipase B from Candida Antartica with Bound Suicide Inhibitor

N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE

Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation.

NAG A 402 HAS WRONG CHIRALITY AT ATOM C1

AAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVGLPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQ
SFDSNWIPLSAQLGYTPCWISPPPFMLNDTQVNTEYMVNAITTLYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVD
RLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFN
GKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSALRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAA

20% PEG 3350, 0.2M SODIUM DIHYDROGEN PHOSPHATE, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K

Structural Consequences of a Circular Permutation on Lipase B from Candida Antartica

THE RECOMBINANT PROTEIN IS A "CIRCULAR PERMUTATION" OF LIPASE B IN WHICH THE C-TERMINAL SEQUENCE AAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP HAS BEEN MOVED TO THE N-TERMINUS WITH THE TP REPLACED WITH G. ALA82 AND THR114 REPRESENT VARIATIONS FROM THE PUBLISHED WILD TYPE SEQUENCE AND THEIR ACCURACY WAS CONFIRMED INDEPENDENTLY BY DNA SEQUENCING

CIRCULAR PERMUTATION, SUICIDE INHIBITION, HYDROLASE, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipid degradation, Zymogen

LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFMLNDTQVNT
EYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTG
SALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSA
LRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAA