Nature Search

Structural basis of latency in plasminogen activator inhibitor-1

James Mottonen
Arne Strand
Elizabeth J. Goldsmith
Research16 Jan 1992
Nature

Volume: 355, P: 270-273
Structure of the collagen-binding ___domain from a Staphylococcus aureus adhesin

Jindrich Symersky
Joseph M. Patti
Sthanam V.L. Narayana
Research01 Oct 1997
Nature Structural Biology

Volume: 4, P: 833-838
Structure of the c₁₀ ring of the yeast mitochondrial ATP synthase in the open conformation

The membrane-embedded c-ring allows the passage of protons to power the synthesis of ATP by the FoF1 ATPase. Previous structural data have shown the proton acceptor-donor sites in a closed, ion-locked conformation. Structural and computational data now reveal the open conformation of the yeast mitochondrial c₁₀ ring.

Jindrich Symersky
Vijayakanth Pagadala
David M Mueller
Research15 Apr 2012
Nature Structural & Molecular Biology

Volume: 19, P: 485-491
Structure and function of the divalent anion/Na⁺ symporter from Vibrio cholerae and a humanized variant

Divalent anion/Na⁺ symporter (DASS) transporters move intermediates of the Krebs cycle across the cell membrane. Here the authors present the substrate-bound structures of VcINDY, a DASS from Vibrio cholerae, which provide insights into the underlying transport mechanism.

Rongxin Nie
Steven Stark
Min Lu
ResearchOpen Access24 Apr 2017
Nature Communications

Volume: 8, P: 1-10
Structural insights into H⁺-coupled multidrug extrusion by a MATE transporter

Bacterial multidrug efflux transporters (MATEs) couple drug export to Na⁺ or H⁺ influx. A new crystal structure of the H⁺-coupled DinF transporter from Bacillus halodurans reveals differences in the substrate-binding sites and transport mechanisms of DinF and NorM MATE homologs.

Min Lu
Martha Radchenko
Yi Guo
Research20 Oct 2013
Nature Structural & Molecular Biology

Volume: 20, P: 1310-1317
Structural basis for the blockade of MATE multidrug efflux pumps

MATE transporters confer bacterial multidrug resistance by transporting drugs across cell membranes. Here, the authors present new structures of the DinF and NorM MATE transporters and reveal insights into the mechanisms of substrate transport and MATE inhibition by small-molecule pharmaceuticals.

Martha Radchenko
Jindrich Symersky
Min Lu
ResearchOpen Access06 Aug 2015
Nature Communications

Volume: 6, P: 1-11
Bedaquiline inhibits the yeast and human mitochondrial ATP synthases

Luo, Zhou et al. show that Bedaquiline (BDQ, Sirturo), approved to treat multi-drug-resistant tuberculosis, inhibits the yeast and human mitochondrial ATP synthases in addition to its intended target, the Mycobacterium tuberculosis ATP synthase. The structure of the mitochondrial ATP synthase bound to BDQ suggests a means to modify this inhibitor to increase its specificity for the M. tuberculosis enzyme, thereby reducing its side effects for patients.

Min Luo
Wenchang Zhou
David M. Mueller
ResearchOpen Access19 Aug 2020
Communications Biology

Volume: 3, P: 1-10
Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily

Hsin-Hui Wu
Jindrich Symersky
Min Lu
ResearchOpen Access03 Mar 2020
Scientific Reports

Volume: 10, P: 1-15
Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition

Hsin-Hui Wu et al. present the structure of the I239T/G354E variant of the MdfA multidrug transporter in complex with three different ligands. They find that this variant has two discrete, non-overlapping substrate binding sites, leading to differential interactions with ligands compared to wild-type MdfA.

Hsin-Hui Wu
Jindrich Symersky
Min Lu
ResearchOpen Access17 Jun 2019
Communications Biology

Volume: 2, P: 1-12

Search

Structural basis of latency in plasminogen activator inhibitor-1

Structure of the collagen-binding ___domain from a Staphylococcus aureus adhesin

Structure of the c₁₀ ring of the yeast mitochondrial ATP synthase in the open conformation

Structure and function of the divalent anion/Na⁺ symporter from Vibrio cholerae and a humanized variant

Structural insights into H⁺-coupled multidrug extrusion by a MATE transporter

Structural basis for the blockade of MATE multidrug efflux pumps

Bedaquiline inhibits the yeast and human mitochondrial ATP synthases

Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily

Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition

Search

Quick links

Search

Filter By:

Search

Quick links