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  • 1.
    Aziz-Qureshi, Abdul
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Meier, Pascal F.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Lee, Chiara
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Drew, David
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    The MEMbrane Protein Single ShoT Amplification Recipe: MemStar2017In: A Structure-Function Toolbox for Membrane Transporter and Channels / [ed] Christine Ziegler, San Diego: Elsevier, 2017, Vol. 594, p. 123-138Chapter in book (Refereed)
    Abstract [en]

    Here, we present a simple overexpression condition for high-throughput screening of membrane proteins in Escherichia coli. For the vast majority of bacterial membrane protein targets tested the MEMbrane protein Single shoT Amplification Recipe-MemStarleads to high production yields of target protein. The use of MemStar has facilitated structural studies of several transport proteins.

  • 2. Lee, Chiara
    et al.
    Kang, Hae Joo
    Hjelm, Anna
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Qureshi, Abdul Aziz
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Nji, Emmanuel
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Choudhury, Hassanul
    Beis, Konstantinos
    de Gier, Jan-Willem
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Drew, David
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Imperial College London, England.
    MemStar: A one-shot Escherichia coli-based approach for high-level bacterial membrane protein production2014In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 588, no 20, p. 3761-3769Article in journal (Refereed)
    Abstract [en]

    Optimising membrane protein production yields in Escherichia coli can be time- and resource-consuming. Here, we present a simple and effective Membrane protein Single shot amplification recipe: MemStar. This one-shot amplification recipe is based on the E. coli strain Lemo21(DE3), the PASM-5052 auto-induction medium and, contradictorily, an IPTG induction step. Using MemStar, production yields for most bacterial membrane proteins tested were improved to reach an average of 5 mg L-1 per OD600 unit, which is significantly higher than yields obtained with other common production strategies. With MemStar, we have been able to obtain new structural information for several transporters, including the sodium/proton antiporter NapA. (C) 2014 Federation of European Biochemical Societies.

  • 3.
    Nji, Emmanuel
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Gulati, Ashutosh
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Qureshi, Abdul Aziz
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Coincon, Mathieu
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Drew, David
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Structural basis for the delivery of activated sialic acid into Golgi for sialyation2019In: Nature Structural & Molecular Biology, ISSN 1545-9993, E-ISSN 1545-9985, Vol. 26, no 6, p. 415-423Article in journal (Refereed)
    Abstract [en]

    The decoration of secretory glycoproteins and glycolipids with sialic acid is critical to many physiological and pathological processes. Sialyation is dependent on a continuous supply of sialic acid into Golgi organelles in the form of CMP-sialic acid. Translocation of CMP-sialic acid into Golgi is carried out by the CMP-sialic acid transporter (CST). Mutations in human CST are linked to glycosylation disorders, and CST is important for glycopathway engineering, as it is critical for sialyation efficiency of therapeutic glycoproteins. The mechanism of how CMP-sialic acid is recognized and translocated across Golgi membranes in exchange for CMP is poorly understood. Here we have determined the crystal structure of a Zea mays CST in complex with CMP. We conclude that the specificity of CST for CMP-sialic acid is established by the recognition of the nucleotide CMP to such an extent that they are mechanistically capable of both passive and coupled antiporter activity.

  • 4. Nomura, Norimichi
    et al.
    Verdon, Gregory
    Kang, Hae Joo
    Shimamura, Tatsuro
    Nomura, Yayoi
    Sonoda, Yo
    Hussien, Saba Abdul
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Qureshi, Aziz Abdul
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Coincon, Mathieu
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Sato, Yumi
    Abe, Hitomi
    Nakada-Nakura, Yoshiko
    Hino, Tomoya
    Arakawa, Takatoshi
    Kusano-Arai, Osamu
    Iwanari, Hiroko
    Murata, Takeshi
    Kobayashi, Takuya
    Hamakubo, Takao
    Kasahara, Michihiro
    Iwata, So
    Drew, David
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Imperial College London, UK.
    Structure and mechanism of the mammalian fructose transporter GLUT52015In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 526, no 7573, p. 397-+Article in journal (Refereed)
    Abstract [en]

    The altered activity of the fructose transporter GLUT5, an isoform of the facilitated-diffusion glucose transporter family, has been linked to disorders such as type 2 diabetes and obesity. GLUT5 is also overexpressed in certain tumour cells, and inhibitors are potential drugs for these conditions. Here we describe the crystal structures of GLUT5 from Rattus norvegicus and Bos taurus in open outward-and open inward-facing conformations, respectively. GLUT5 has a major facilitator superfamily fold like other homologous monosaccharide transporters. On the basis of a comparison of the inward-facing structures of GLUT5 and human GLUT1, a ubiquitous glucose transporter, we show that a single point mutation is enough to switch the substrate-binding preference of GLUT5 from fructose to glucose. A comparison of the substrate-free structures of GLUT5 with occluded substrate-bound structures of Escherichia coli XylE suggests that, in addition to global rocker-switch-like re-orientation of the bundles, local asymmetric rearrangements of carboxy-terminal transmembrane bundle helices TM7 and TM10 underlie a 'gated-pore' transport mechanism in such monosaccharide transporters.

  • 5.
    Qureshi, Abdul Aziz
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Establishing the mechanistic basis of sugar transport2019Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Sugar is a vital molecule required for cell viability and homeostasis. Sugar is important for metabolic energy, energy storage, signaling, structure and osmolyte regulation. Transport of sugar represents an important physiological process. Specific membrane transporter families have evolved to mediate the transport of sugar across biological membranes. In this thesis, we describe our work leading to a better mechanistic understanding of two sugar transporter families, namely glucose (GLUT) transporters and nucleotide-sugar (NST) transporters.

    Members of GLUT transporters, belonging to the Solute Carrier (SLC2) family, are involved in the uptake of various monosaccharides across the cellular membranes. Activity of different NSTs, belonging to the (SLC35) family, is crucial for the process of glycosylation by mediating the translocation of activated sugars from the cytoplasm into the lumen of either Golgi and/or ER organelles. GLUTs and NSTs families carry out transport processes fundamental to human physiology and pathophysiology. Despite the profound importance of GLUTs and NSTs in human health, comprehensive understanding of their architecture and mechanistic features with respect to determinants of substrate binding and allosteric coupling at the molecular level has remained elusive.

    In this thesis, we address key functional and structural properties of GLUT and NST mediated sugar transport. We combine crystal structures with robust binding and transport assays as well as computational approaches. The role of lipids in fine-tuning the activity of transporters is also exemplified by demonstrating the effect of lipid composition in the transport activity of GLUTs using in-vitro proteoliposome assays. Our work has not only enhanced the current understanding of GLUT and NST function, but also developed themes and methods that are likely relevant to many types of small molecule transporters.

  • 6.
    Qureshi, Abdul Aziz
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Suades, Albert
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Matsuoka, Rei
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Brock, Joseph
    McComas, Sarah
    Nji, Emmanuel
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Orellana, Laura
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Claesson, Magnus
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Delemotte, Lucie
    Drew, David
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Malarial parasite transporter structure reveals the molecular basis for sugar importManuscript (preprint) (Other academic)
  • 7.
    Qureshi, Abdul Aziz
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Suades, Albert
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    McComas, Sarah
    Delemotte, Lucie
    Drew, David
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Lipids shape the flat energetic landscape of the GLUT transporter cycleManuscript (preprint) (Other academic)
1 - 7 of 7
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