NDLI: Thermodynamic Evidence for Conformational Coupling between the B and C Domains of the Mannitol Transporter of Escherichia coli, Enzyme IImtl

Content Provider	Journal of Biological Chemistry (JBC)
Author	Meijberg, Wim Schuurman-Wolters, Gea K. Robillard, George T.
Abstract	The transport across the cytoplasmic membrane and concomitant phosphorylation of mannitol in Escherichia coliis catalyzed by the mannitol-specific transport protein from the phosphoenolpyruvate-dependent phosphotransferase system, enzyme IImtl. Interactions between the cytoplasmic B and the membrane embedded C domain play an important role in the catalytic cycle of this enzyme, but the nature of this interaction is largely unknown. We have studied the thermodynamics of binding of (i) mannitol to enzyme IImtl, (ii) the substrate analog perseitol to enzyme IImtl, (iii) perseitol to phosphorylated enzyme IImtl, and (iv) mannitol to enzyme IImtltreated with trypsin to eliminate the cytoplasmic domains. Analysis of the heat capacity increment of these reactions showed that approximately 50–60 residues are involved in the binding of mannitol and perseitol, but far less in the phosphorylated state or after removal of the B domain. A model is proposed in which binding of mannitol leads to the formation of a contact interface between the two domains, either by folding of unstructured parts or by docking of preexisting surfaces, thus positioning the incoming mannitol close to the phosphorylation site on the B domain to facilitate the transfer of the phosphoryl group.
Related Links	http://www.jbc.org/content/273/14/7949.abstract
Ending Page	7956
Starting Page	7949
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	14
Volume Number	273
DOI	10.1074/jbc.273.14.7949
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1998-04-03
Access Restriction	Open
Subject Keyword	MEMBRANES AND BIOENERGETICS
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Thermodynamic evidence for conformational coupling between the B and C domains of the mannitol transporter of Escherichia coli, Enzyme IImtl (1998)

Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli: Physical size of enzyme IImtl and its domains IIBA and IIC in the active state

The membrane-bound domain of the phosphotransferase enzyme IImtl of Escherichia coli constitutes a mannitol translocating unit

Phosphorylation site mutants of the mannitol transport protein enzyme IImtl of Escherichia coli: studies on the interaction between the mannitol translocating C-domain and the phosphorylation site on the energy-coupling B-domain.

Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.

A Mutation in the Escherichia coliF0F1-ATP Synthase Rotor, γE208K, Perturbs Conformational Coupling between Transport and Catalysis

Membrane Insertion Characteristics of the Various Transmembrane Domains of the Escherichia coli TolQ Protein

Purification by Ni2+ Affinity Chromatography, and Functional Reconstitution of the Transporter for N-Acetylglucosamine of Escherichia coli

Solution Structure of a Post-transition State Analog of the Phosphotransfer Reaction between the A and B Cytoplasmic Domains of the Mannitol Transporter IIMannitol of the Escherichia coli Phosphotransferase System

Thermodynamic Evidence for Conformational Coupling between the B and C Domains of the Mannitol Transporter of Escherichia coli, Enzyme IImtl

Similar Documents

Thermodynamic evidence for conformational coupling between the B and C domains of the mannitol transporter of Escherichia coli, Enzyme IImtl (1998)

Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli: Physical size of enzyme IImtl and its domains IIBA and IIC in the active state

The membrane-bound domain of the phosphotransferase enzyme IImtl of Escherichia coli constitutes a mannitol translocating unit

Phosphorylation site mutants of the mannitol transport protein enzyme IImtl of Escherichia coli: studies on the interaction between the mannitol translocating C-domain and the phosphorylation site on the energy-coupling B-domain.

Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.

A Mutation in the Escherichia coliF0F1-ATP Synthase Rotor, γE208K, Perturbs Conformational Coupling between Transport and Catalysis

Membrane Insertion Characteristics of the Various Transmembrane Domains of the Escherichia coli TolQ Protein

Purification by Ni2+ Affinity Chromatography, and Functional Reconstitution of the Transporter for N-Acetylglucosamine of Escherichia coli

Solution Structure of a Post-transition State Analog of the Phosphotransfer Reaction between the A and B Cytoplasmic Domains of the Mannitol Transporter IIMannitol of the Escherichia coli Phosphotransferase System

Thermodynamic Evidence for Conformational Coupling between the B and C Domains of the Mannitol Transporter of Escherichia coli, Enzyme IImtl