6LGY

Crystal structure of a cysteine-pair mutant (P10C-S291C) of a bacterial bile acid transporter in an inward-facing state complexed with glycine and sodium

Summary for 6LGY

• Entry DOI: 10.2210/pdb6lgy/pdb
• Related: 6LGV
• Descriptor: Transporter, sodium/bile acid symporter family, GLYCINE, SODIUM ION, ... (6 entities in total)
• Functional Keywords: bile acid transporter, asbt, ntcp, slc10, transport protein
• Biological source: Yersinia frederiksenii
• Total number of polymer chains: 1
• Total formula weight: 34279.97

Authors

Wang, X.,Lyu, Y.,Ji, Y.,Sun, Z.,Zhou, X. (deposition date: 2019-12-06, release date: 2020-12-09, Last modification date: 2024-10-23)

Primary citation

Wang, X.,Lyu, Y.,Ji, Y.,Sun, Z.,Zhou, X.
Substrate binding in the bile acid transporter ASBT Yf from Yersinia frederiksenii.
Acta Crystallogr D Struct Biol, 77:117-125, 2021

PubMed Abstract: Apical sodium-dependent bile acid transporter (ASBT) retrieves bile acids from the small intestine and plays a pivotal role in enterohepatic circulation. Currently, high-resolution structures are available for two bacterial ASBT homologs (ASBT from Neisseria meningitides and ASBT from Yersinia frederiksenii), from which an elevator-style alternating-access mechanism has been proposed for substrate transport. A key concept in this model is that the substrate binds to the central cavity of the transporter so that the elevator-like motion can expose the bound substrate alternatingly to either side of the membrane during a transport cycle. However, no structure of an ASBT has been solved with a substrate bound in its central cavity, so how a substrate binds to ASBT remains to be defined. In this study, molecular docking, structure determination and functional analysis were combined to define and validate the details of substrate binding in ASBT. The findings provide coherent evidence to provide a clearer picture of how the substrate binds in the central cavity of ASBT that fits the alternating-access model.

PubMed: 33404531
DOI: 10.1107/S2059798320015004

Experimental method

X-RAY DIFFRACTION (2.247 Å)