Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Glu

(E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid

Structural studies reveal flexible roof of active site responsible for omega-transaminase CrmG overcoming by-product inhibition.

MTHPSGEPVYADAVLNGWLTSMGLGVEYVRAEGNTVYYLDDEGREVPVLDHACGFGSLIFGHNHPEIIAHAKAALDAGTV
VHAQLSRQPRANQISRILNDIMRRETGRDDRYNAIFANSGAEANEICMKHAELERQERITALFAEIDAELDTAREALTTG
TATLDTASLPLVGGGAGDVDGVIADIHRHNDERRAERPLFLTLDGSFHGKLVGSIQLTQNEPWRTPFTALSSPARFLPAD
EPELIGKIVEDERRSVLTLSLDKDTVRVVERDFPVVAAIFVEPVRGGSGMKTVTPELAEELHRLRDTLGCPLVVDEVQTG
IGRTGAFFGSALLGIRGDYYTLAKAIGGGIVKNSVALIRQDRFLPAMEVIHSSTFAKDGLSASIALKVLEMVEADGGRVY
QRVRERGQRLEAMLESVRADHSDVVSAVWGTGLMLALELRDQSNATSQAIREKAAHGFLGYVLAGFLLREHHIRVLPAGP
RSGFLRFSPSLYITDEEIDRTETALRSLFTALRDQDGDRLVLS

0.2M Sodium acetate, 0.1M TRIS pH 8.5, 32% PEG 3350, 2% glycerol

National Natural Science Foundation of China

SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/F_PLUS COLUMNS.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY

aminotransferase, CrmG, Amino donor, TRANSFERASE