NMR structure of the IIAchitobiose-IIBchitobiose phosphoryl transition state complex of the N,N'-diacetylchitoboise brance of the E. coli phosphotransferase system.

Solution Structure of the Iiachitobose-Iibchitobiose Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia Coli Phosphotransfer System

Solution Structure of Enzyme Iia(Chitobiose) from the N,N'-Diacetylchitobiose Branch of the Escherichia Coli Phosphotransferase System.

The Structure of an Energy-Coupling Protein from Bacteria, Iibcellobiose, Reveals Similarity to Eukaryotic Protein Tyrosine Phosphatases.

NMR Structure of Cysteinyl-Phosphorylated Enzyme Iib of the N,N'-Diacetylchitobiose-Specific Phosphoenolpyruvate-Dependent Phosphotransferase System of Escherichia Coli.

N\,N'-DIACETYLCHITOBIOSE-SPECIFIC PHOSPHOTRANSFERASE ENZYME IIA COMPONENT

N\,N'-DIACETYLCHITOBIOSE-SPECIFIC PHOSPHOTRANSFERASE ENZYME IIB COMPONENT

IIACHB, PTS SYSTEM N\,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIA COMPONENT, EIIA-CHB, EIII-CHB

IIBCHB, PTS SYSTEM N\,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIB COMPONENT

AEELEEVVMGLIINSGQARSLAYAALKQAKQGDFAAAKAMMDQSRMALNEAHLVQTKLIEGDAGEGKMKVSLVLVHAQLH
LMTSMLARELITELIELHEKLKA

KKHIYLFCSAGMSTSLLVSKMRAQAEKYEVPVIIEAFPETLAGEKGQNADVVLLGPQIAYMLPEIQRLLPNKPVEVIDSL
LYGKVDGLGVLKAAVAAIKKAAA

NMR STRUCTURE OF THE IIACHITOBIOSE- IIBCHITOBIOSE COMPLEX OF THE N,N'- DIACETYLCHITOBOISE BRANCE OF THE E. COLI PHOSPHOTRANSFERASE SYSTEM.

TRIMERIC STRUCTURE OF THE ENZYME IIA FROM ESCHERICHIA COLI PHOSPHOTRANSFERASE SYSTEM SPECIFIC FOR N,N'-DIACETYLCHITOBIOSE

ENGINEERED RESIDUE IN CHAIN A, ASP 92 TO LEU ENGINEERED RESIDUE IN CHAIN B, ASP 92 TO LEU ENGINEERED RESIDUE IN CHAIN C, ASP 92 TO LEU
PHOSPHORYL GROUP (PO3): THIS IS A PLANAR PHOSPHORYL GROUP IN A PENTACOORDINATE TRANSITION STATE

RESIDUE 1 IN CHAINS A, B AND C CORRESPONDS TO RESIDUE 14
OF WILD TYPE IIACHB, RESIDUE 76 IS A HIS.
TO OBTAIN WILD TYPE NUMBERING ADD 14. IN THE CONSTRUCT
EMPLOYED THE 1ST 13 RESIDUES OF THE WILD TYPE HAVE BEEN
DELETED.
CHAIN D SEQUENCE STARTS AT RESIDUE 3
CHAIN D BEST MATCH AGAINST UNIPROT SEQUENCE DATABASE WAS
FOUND TO BE C3T7F7. CHAIN D IS CHEMICALLY SYNTHESIZED.

THE STRUCTURE WAS SOLVED ON THE BASIS OF THE COORDINATES OF THE UNPHOSPHORYLATED COMPLEX 2WWV. TO SOLVE THE TRANSITION STATE COMPLEX, THE COORDINATES OF THE UNPHOSPHORYLATED COMPLEX 2WWV ARE HELD FIXED WITH THE EXCEPTION OF THE ACTIVE SITE LOOP OF IIBCHB, THE ACTIVE SITE OF IIACHB, THE PHOSPHORYL GROUP, AND INTERFACIAL SIDE CHAINS IN THE IMMEDIATE VICINITY OF THE ACTIVE SITE AND THE PHOSPHORYL GROUP WHICH ARE GIVEN TORSION DEGREES OF FREEDOM. THE ACTIVE SITE LOOP OF IIBCHB COMPRISES RESIDUES 9-16 OF CHAIN D. THE ACTIVE SITE REGION OF IIACHB COMPRISES RESIDUES 74 TO 79 OF CHAINS A, B AND C. THE EXPERIMENTAL NMR RESTRAINTS ARE IDENTICAL TO THOSE USED TO CALCULATE 2WWV EXCEPT FOR THE DIPOLAR COUPLINGS WHICH WERE OBTAINED FROM FREE PHOSPHORYLATED IIBCHB. FOR FURTHER DETAILS SEE THE JNRL CITATION ABOVE.

KINASE, PHOSPHOTRANSFERASE SYSTEM, CHITOBIOSE, TRANSFERASE, SUGAR TRANSPORT