Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases

Kim, Hyoun Sook; Lee, Sang Jae; Yoon, Hye Jin; An, Doo Ri; Kim, Dojin; Kim, Soon-Jong; Suh, Se Won

doi:10.1016/j.jsb.2011.05.007

Cited by 24 publications

(37 citation statements)

References 33 publications

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“…Mutations in residues in the conserved histidines or aspartic acids have been demonstrated to result in a loss of activity for CpsB (28), its homolog Wzb in Lactobacillus rhamnosus (not to be confused with Gram-negative Wzb) (15), and its B. subtilis homolog, YwqE (17). The crystal structures of the S. pneumoniae CPS serotype 4 enzyme Cps4B confirmed the importance of these conserved histidines for CpsB activity while demonstrating that two additional non-PHP motif residues, glutamic acids at positions 80 and 108, are also integral to CpsB activity (32,33). Two arginine residues, one each in motifs 3 and 4, were demonstrated to be directly involved in phosphotyrosine binding (32).…”

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confidence: 79%

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Streptococcus pneumoniae Phosphotyrosine Phosphatase CpsB and Alterations in Capsule Production Resulting from Changes in Oxygen Availability

Geno¹,

Hauser²,

Gupta³

et al. 2014

Journal of Bacteriology

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Streptococcus pneumoniae produces a protective capsular polysaccharide whose production must be modulated for bacterial survival within various host niches. Capsule production is affected in part by a phosphoregulatory system comprised of CpsB, CpsC, and CpsD. Here, we found that growth of serotype 2 strain D39 under conditions of increased oxygen availability resulted in decreased capsule levels concurrent with an ϳ5-fold increase in Cps2B-mediated phosphatase activity. The change in Cps2B phosphatase activity did not result from alterations in the levels of either the cps2B transcript or the Cps2B protein. Recombinant Cps2B expressed in Escherichia coli similarly exhibited increased phosphatase activity under conditions of high-oxygen growth. S. pneumoniae D39 derivatives with defined deletion or point mutations in cps2B demonstrated reduced phosphatase activity with corresponding increases in levels of Cps2D tyrosine phosphorylation. There was, however, no correlation between these phenotypes and the level of capsule production. During growth under reduced-oxygen conditions, the Cps2B protein was essential for parental levels of capsule, but phosphatase activity alone could be eliminated without an effect on capsule. Under increased-oxygen conditions, deletion of cps2B did not affect capsule levels. These results indicate that neither Cps2B phosphatase activity nor Cps2D phosphorylation levels per se are determinants of capsule levels, whereas the Cps2B protein is important for capsule production during growth under conditions of reduced but not enhanced oxygen availability. Roles for factors outside the capsule locus, possible interactions between capsule regulatory proteins, and links to other cellular processes are also suggested by the results described in this study.

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confidence: 79%

“…Unlike low-molecular-weight phosphotyrosine phosphatases, which utilize a catalytic cysteine residue in their active sites (30,31), PHP proteins utilize a series of coordinated histidine and aspartic acid residues in their catalysis (15,17,29,(32)(33)(34). These residues are coordinated through four characteristic PHP motifs (29).…”

mentioning

confidence: 99%

Streptococcus pneumoniae Phosphotyrosine Phosphatase CpsB and Alterations in Capsule Production Resulting from Changes in Oxygen Availability

Geno¹,

Hauser²,

Gupta³

et al. 2014

Journal of Bacteriology

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“…In bacteria, most tyrosine phosphatases belong to the cysteinebased low-molecular-mass phosphotyrosine phosphatase (LMPTP) family (Vincent et al, 1999) or polymerase and histidinol phosphatase (PHP) family (Aravind & Koonin, 1998). LMPTPs and PHPs have completely different structures (Hagelueken et al, 2009;Kim et al, 2011). LMPTPs characteristically function via a conserved cysteine residue that serves as a nucleophile.…”

Section: Introductionmentioning

confidence: 99%

“…PHPs have been mostly found in Gram-positive bacteria, and PHPs are divalent metal ion-dependent phosphotyrosine phosphatases. The active site of both YwqE and CpsB, which belong to the PHP family, contains a cluster of three metal ions binding to phosphate (Kim et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

PhpA, a tyrosine phosphatase of Myxococcus xanthus, is involved in the production of exopolysaccharide

et al. 2012

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Protein-tyrosine phosphorylation plays a significant role in multiple cellular functions in bacteria. Bacterial tyrosine phosphatases catalyse the dephosphorylation of tyrosyl-phosphorylated proteins. Myxococcus xanthus PhpA shares homology with DNA polymerase and histidinol phosphatase family members. Recombinant His-tagged PhpA requires Mn 2+ or Co 2+ for phosphatase activity, and shows strict specificity for phosphorylated tyrosine residues. The k m values of PhpA for p-nitrophenyl phosphate (pNPP) and phosphotyrosine peptide, RRLIEDAEpYAARG, were 803 and 139 mM, respectively. The phosphatase activity of PhpA was inhibited by sodium orthovanadate with a k i of 33 mM. phpA gene expression was observed under both vegetative and developmental conditions, but peaked during late fruiting body formation. A phpA mutant exhibited an elevated level of tyrosine phosphorylation of a 79 kDa protein and cytoplasmic tyrosine kinase, BtkA. In M. xanthus, exopolysaccharide (EPS) is essential for cellcell adhesion and fruiting body formation. phpA mutant cells exhibited enhanced capacity for cellcell agglutination in agglutination buffer. Under starvation conditions, phpA mutation caused early aggregation and sporulation. The EPS production assay showed that the phpA mutant produced an increased amount of EPS in comparison with the wild-type. These results indicate that PhpA may negatively regulate the production of EPS in M. xanthus.

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“…Thus, this would suggest that while these two phosphatases are relatively divergent, they share some similarity in their active sites. Recently, the structure of YwqE, a phosphatase from the Gram-positive bacterium Bacillus subtilis was solved [89].…”

Section: Regulationmentioning

confidence: 99%

Wzy-Dependent Bacterial Capsules as Potential Drug Targets

Ericsson

Standish²,

Kobe³

et al. 2012

CDT

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Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases

Cited by 24 publications

References 33 publications

Streptococcus pneumoniae Phosphotyrosine Phosphatase CpsB and Alterations in Capsule Production Resulting from Changes in Oxygen Availability

Streptococcus pneumoniae Phosphotyrosine Phosphatase CpsB and Alterations in Capsule Production Resulting from Changes in Oxygen Availability

PhpA, a tyrosine phosphatase of Myxococcus xanthus, is involved in the production of exopolysaccharide

Wzy-Dependent Bacterial Capsules as Potential Drug Targets

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