2010
DOI: 10.1074/jbc.m110.135434
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The Sortase A Enzyme That Attaches Proteins to the Cell Wall of Bacillus anthracis Contains an Unusual Active Site Architecture

Abstract: The pathogen Bacillus anthracis uses the Sortase A (SrtA) enzyme to anchor proteins to its cell wall envelope during vegetative growth. To gain insight into the mechanism of protein attachment to the cell wall in B. anthracis we investigated the structure, backbone dynamics, and function of SrtA. The NMR structure of SrtA has been determined with a backbone coordinate precision of 0.40 ؎ 0.07 Å . SrtA possesses several novel features not previously observed in sortase enzymes including the presence of a struct… Show more

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Cited by 59 publications
(66 citation statements)
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“…The LPXTG motif is conserved in a wide variety of surface proteins (35); however, the chemical structure of the peptidoglycan crossbridge varies between different bacterial species (36). Although structurally similar (37)(38)(39)(40), the amino acid identity between sortases from different Gram-positive bacteria is limited to a few key residues at or near the active site (34). We therefore asked whether compound 6e can inhibit sortase from three different microbes: Bacillus anthracis, Streptococcus pneumoniae, and Streptococcus pyogenes.…”
Section: Resultsmentioning
confidence: 99%
“…The LPXTG motif is conserved in a wide variety of surface proteins (35); however, the chemical structure of the peptidoglycan crossbridge varies between different bacterial species (36). Although structurally similar (37)(38)(39)(40), the amino acid identity between sortases from different Gram-positive bacteria is limited to a few key residues at or near the active site (34). We therefore asked whether compound 6e can inhibit sortase from three different microbes: Bacillus anthracis, Streptococcus pneumoniae, and Streptococcus pyogenes.…”
Section: Resultsmentioning
confidence: 99%
“…Mutations were made using the QuikChange method (Agilent, San Diego, CA) and confirmed by DNA sequencing. Mutants, wild-type Ba SrtA (amino acid residues Asp 57 -Lys 210 ), and wild-type Ba SrtA ⌬64 (amino acid residues Asp 65 -Lys 210 ) were purified as described previously (23). In vitro substrate hydrolysis assay was performed as previously described (57).…”
Section: Cmentioning
confidence: 99%
“…However, it is not well understood how sortases recognize their sorting signal and nucleophile substrates, because nearly all sortase structures reported to date have been determined in the apo-state. Previously we discovered that the class A Ba SrtA sortase contains a unique N-terminal appendage that wraps around the body of the protein to contact the active site of the enzyme (23). However, the function of this appendage in catalysis remained unknown.…”
mentioning
confidence: 99%
“…Sortases typically harbor a conserved histidine and a TLXTC motif in their active sites, in which replacement of the single conserved cysteine with alanine has been shown to abolish enzyme activity in Staphylococcus aureus (2). Based on primary sequences and substrate specificities, sortases are grouped into four classes (A to D), of which sortase A (SrtA) is referred to as the housekeeping sortase (3,4). The role of SrtA in surface protein sorting was initially described in S. aureus (5,6), where it was found to recognize proteins bearing the conserved C-terminal cell wall sorting signal LPXTG (7).…”
mentioning
confidence: 99%