2009
DOI: 10.1074/jbc.m109.049635
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A Mycobacterial Cyclic AMP Phosphodiesterase That Moonlights as a Modifier of Cell Wall Permeability

Abstract: Mycobacterium tuberculosis utilizes many mechanisms to establish itself within the macrophage, and bacterially derived cAMP is important in modulating the host cellular response. Although the genome of M. tuberculosis is endowed with a number of mammalian-like adenylyl cyclases, only a single cAMP phosphodiesterase has been identified that can decrease levels of cAMP produced by the bacterium. We present the crystal structure of the full-length and sole cAMP phosphodiesterase, Rv0805, found in M. tuberculosis,… Show more

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Cited by 67 publications
(123 citation statements)
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References 33 publications
(59 reference statements)
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“…Swapped structural elements were constituted largely by the C terminus of the protein (Leu 266 -Ile 290 ), placed at the entrance of the active site. Electron density for amino acids of the C terminus beyond Asp 298 was not observed in the crystal structure of Rv0805, indicating that this region was flexible (17). Interestingly, residues Pro 278 -Asp 318 of the C terminus of Rv0805 (henceforth referred to as the C-terminal extension (CTE)) do not bear sequence similarity to other MPEs, suggesting regulatory roles relevant in vivo rather than being involved in catalysis.…”
Section: Metallophosphoesterases (Mpes)mentioning
confidence: 98%
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“…Swapped structural elements were constituted largely by the C terminus of the protein (Leu 266 -Ile 290 ), placed at the entrance of the active site. Electron density for amino acids of the C terminus beyond Asp 298 was not observed in the crystal structure of Rv0805, indicating that this region was flexible (17). Interestingly, residues Pro 278 -Asp 318 of the C terminus of Rv0805 (henceforth referred to as the C-terminal extension (CTE)) do not bear sequence similarity to other MPEs, suggesting regulatory roles relevant in vivo rather than being involved in catalysis.…”
Section: Metallophosphoesterases (Mpes)mentioning
confidence: 98%
“…The structure of Rv0805 shows a canonical MPE-like-fold, with a surface-exposed active site with bound Fe 3ϩ and Mn 2ϩ ions (17,18). Docking studies with 3Ј,5Ј-cAMP, 2Ј,3Ј-cAMP, and bispNPP as well as co-crystallization with 5Ј-AMP identified interactions between active site metals and phosphate moieties as contributing to the primary recognition between Rv0805 and its substrates, partially explaining the observed promiscuous substrate utilization (17).…”
Section: Metallophosphoesterases (Mpes)mentioning
confidence: 99%
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