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Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

Author

Listed:
  • Martín Alcorlo

    (Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)

  • David A. Dik

    (University of Notre Dame, Notre Dame)

  • Stefania Benedetti

    (University of Notre Dame, Notre Dame)

  • Kiran V. Mahasenan

    (University of Notre Dame, Notre Dame)

  • Mijoon Lee

    (University of Notre Dame, Notre Dame)

  • Teresa Domínguez-Gil

    (Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)

  • Dusan Hesek

    (University of Notre Dame, Notre Dame)

  • Elena Lastochkin

    (University of Notre Dame, Notre Dame)

  • Daniel López

    (Spanish National Research Council (CNB-CSIC))

  • Bill Boggess

    (University of Notre Dame, Notre Dame)

  • Shahriar Mobashery

    (University of Notre Dame, Notre Dame)

  • Juan A. Hermoso

    (Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)

Abstract

SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is enriched in the septal ring as a product of catalysis by cell-wall amidases that participate in the separation of daughter cells during cell division. Here, we document binding of synthetic denuded glycan ligands to the SPOR domain of the lytic transglycosylase RlpA from Pseudomonas aeruginosa (SPOR-RlpA) by mass spectrometry and structural analyses, and demonstrate that indeed the presence of peptide stems in the peptidoglycan abrogates binding. The crystal structures of the SPOR domain, in the apo state and in complex with different synthetic glycan ligands, provide insights into the molecular basis for recognition and delineate a conserved pattern in other SPOR domains. The biological and structural observations presented here are followed up by molecular-dynamics simulations and by exploration of the effect on binding of distinct peptidoglycan modifications.

Suggested Citation

  • Martín Alcorlo & David A. Dik & Stefania Benedetti & Kiran V. Mahasenan & Mijoon Lee & Teresa Domínguez-Gil & Dusan Hesek & Elena Lastochkin & Daniel López & Bill Boggess & Shahriar Mobashery & Juan A, 2019. "Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13354-4
    DOI: 10.1038/s41467-019-13354-4
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    Cited by:

    1. Zhixin Lyu & Atsushi Yahashiri & Xinxing Yang & Joshua W. McCausland & Gabriela M. Kaus & Ryan McQuillen & David S. Weiss & Jie Xiao, 2022. "FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Adrian Izquierdo-Martinez & Maria Billini & Vega Miguel-Ruano & Rogelio Hernández-Tamayo & Pia Richter & Jacob Biboy & María T. Batuecas & Timo Glatter & Waldemar Vollmer & Peter L. Graumann & Juan A., 2023. "DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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