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4IIP

Legionella pneumophila effector

Summary for 4IIP
Entry DOI10.2210/pdb4iip/pdb
Related4IIK
DescriptorAdenosine monophosphate-protein hydrolase SidD, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsbeta sandwich, de-ampylation, rab1, legionella containing vacuole surface, hydrolase
Biological sourceLegionella pneumophila
Cellular locationHost cytoplasm, host perinuclear region: Q5ZSQ2
Total number of polymer chains1
Total formula weight37022.05
Authors
Tascon, I.,Chen, Y.,Neunuebel, M.R.,Rojas, A.L.,Machner, M.P.,Hierro, A. (deposition date: 2012-12-20, release date: 2013-06-19, Last modification date: 2024-03-20)
Primary citationChen, Y.,Tascon, I.,Neunuebel, M.R.,Pallara, C.,Brady, J.,Kinch, L.N.,Fernandez-Recio, J.,Rojas, A.L.,Machner, M.P.,Hierro, A.
Structural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidD
Plos Pathog., 9:e1003382-e1003382, 2013
Cited by
PubMed Abstract: The covalent attachment of adenosine monophosphate (AMP) to proteins, a process called AMPylation (adenylylation), has recently emerged as a novel theme in microbial pathogenesis. Although several AMPylating enzymes have been characterized, the only known virulence protein with de-AMPylation activity is SidD from the human pathogen Legionella pneumophila. SidD de-AMPylates mammalian Rab1, a small GTPase involved in secretory vesicle transport, thereby targeting the host protein for inactivation. The molecular mechanisms underlying Rab1 recognition and de-AMPylation by SidD are unclear. Here, we report the crystal structure of the catalytic region of SidD at 1.6 Å resolution. The structure reveals a phosphatase-like fold with additional structural elements not present in generic PP2C-type phosphatases. The catalytic pocket contains a binuclear metal-binding site characteristic of hydrolytic metalloenzymes, with strong dependency on magnesium ions. Subsequent docking and molecular dynamics simulations between SidD and Rab1 revealed the interface contacts and the energetic contribution of key residues to the interaction. In conjunction with an extensive structure-based mutational analysis, we provide in vivo and in vitro evidence for a remarkable adaptation of SidD to its host cell target Rab1 which explains how this effector confers specificity to the reaction it catalyses.
PubMed: 23696742
DOI: 10.1371/journal.ppat.1003382
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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數據於2024-11-06公開中

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