1E2A

ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS

Summary for 1E2A

• Entry DOI: 10.2210/pdb1e2a/pdb
• Descriptor: ENZYME IIA, MAGNESIUM ION (3 entities in total)
• Functional Keywords: enzyme iia, helical bundles, pts, transferase, phosphotransferase system
• Biological source: Lactococcus lactis
• Cellular location: Cytoplasm: P23532
• Total number of polymer chains: 3
• Total formula weight: 34413.66

Authors

Sliz, P.,Engelmann, R.,Hengstenberg, W.,Pai, E.F. (deposition date: 1997-04-25, release date: 1998-04-29, Last modification date: 2024-02-07)

Primary citation

Sliz, P.,Engelmann, R.,Hengstenberg, W.,Pai, E.F.
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
Structure, 5:775-788, 1997

PubMed Abstract: The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the binding, transmembrane transport and phosphorylation of numerous sugar substrates. The system is also involved in the regulation of a variety of metabolic and transcriptional processes. The PTS consists of two non-specific energy coupling components, enzyme I and a heat stable phosphocarrier protein (HPr), as well as several sugar-specific multiprotein permeases known as enzymes II. In most cases, enzymes IIA and IIB are located in the cytoplasm, while enzyme IIC acts as a membrane channel. Enzyme IIAlactose belongs to the lactose/cellobiose-specific family of enzymes II, one of four functionally and structurally distinct groups. The protein, which normally functions as a trimer, is believed to separate into its subunits after phosphorylation.

PubMed: 9261069
DOI: 10.1016/S0969-2126(97)00232-3

Experimental method

X-RAY DIFFRACTION (2.3 Å)