2GPR

GLUCOSE PERMEASE IIA FROM MYCOPLASMA CAPRICOLUM

Summary for 2GPR

• Entry DOI: 10.2210/pdb2gpr/pdb
• Descriptor: GLUCOSE-PERMEASE IIA COMPONENT (2 entities in total)
• Functional Keywords: phosphotransferase, glucose permease, enzyme iia, mycoplasma
• Biological source: Mycoplasma capricolum
• Cellular location: Cytoplasm: P45618
• Total number of polymer chains: 1
• Total formula weight: 16723.24

Authors

Huang, K.,Herzberg, O. (deposition date: 1998-05-19, release date: 1998-08-12, Last modification date: 2024-05-29)

Primary citation

Huang, K.,Kapadia, G.,Zhu, P.P.,Peterkofsky, A.,Herzberg, O.
A promiscuous binding surface: crystal structure of the IIA domain of the glucose-specific permease from Mycoplasma capricolum.
Structure, 6:697-710, 1998

PubMed Abstract: The phosphoenolpyruvate:sugar phosphotransferase system (PTS) is a bacterial and mycoplasma system responsible for the uptake of some sugars, concomitant with their phosphorylation. The sugar-specific component of the system, enzyme II (EII),consists of three domains, EIIA, EIIB and EIIC. EIIA and ELLB are cytoplasmic and EIIC is an integral membrane protein that contains the sugar-binding site. Phosphoenolpyruvate (PEP) provides the source of the phosphoryl group, which is transferred via several phosphoprotein intermediates, eventually being transferred to the internalized sugar. Along the pathway, EIIA accepts a phosphoryl group from the phosphocarrier protein HPr and transfers it to EIIB. The structure of the glucose-specific EIIA (EIIAglc) from Mycoplasma capricolum reported here facilitates understanding of the nature of the interactions between this protein and its partners.

PubMed: 9705652
DOI: 10.1016/S0969-2126(98)00072-0

Experimental method

X-RAY DIFFRACTION (2.5 Å)