Crystal structure of a secretory signalling glycoprotein from sheep at 2.0 Å resolution

Srivastava, Divya; Ethayathulla, A.S.; Kumar, Janesh; Singh, Nagendra; Sharma, Sujata; Das, Utpal; Srinivasan, Alagiri

doi:10.1016/j.jsb.2006.05.008

Cited by 24 publications

(31 citation statements)

References 33 publications

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“…Pathway analysis implicated decreased CHI3L-1 expression in the predicted reduction in cell death in response to 4ϫ milking. In agreement, CHI3L-1, which is a secreted protein, has been previously reported to be upregulated during mammary involution and remodeling in dairy cows (28,44), goats (29,40), and sheep (46). More recently, differential expression of CHI3L-1 mRNA was linked to lactogenic changes in mammary cells in culture (47).…”

Section: Response To 4ϫ Milking: Genes and Functionssupporting

confidence: 63%

Acute milk yield response to frequent milking during early lactation is mediated by genes transiently regulated by milk removal

Wall

Bond

McFadden

2012

Physiological Genomics

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Section: Response To 4ϫ Milking: Genes and Functionssupporting

confidence: 63%

Acute milk yield response to frequent milking during early lactation is mediated by genes transiently regulated by milk removal

Wall

Bond

McFadden

2012

Physiological Genomics

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“…Ala substitutions of conserved residues in the C-terminal domain of HmsF, the Yersinia pestis homolog of PgaB, had no effect on biofilm formation (33), further supporting the idea that PgaB 310-672 may be acting as a carbohydrate binding domain. Whereas the dissociation constant of PgaB 310-672 for β-1,6-(GlcNAc) 6 is weaker than those observed for chi-lectins, which have K d values for β-1,4-(GlcNAc) 6 (chitohexaose) in the low (<20 μM) range (26)(27)(28)(29)(30), stronger interactions may be observed with longer or partially de-N-acetylated PNAG oligomers. The simulation data support this notion because β-D-GlcNH 3 + density is only located along the electronegative groove of PgaB 310-672 , suggesting the domain may preferentially bind dPNAG ( Fig.…”

Section: Discussionmentioning

confidence: 81%

“…A number of GH18 members (chi-lectins) with mutations in the catalytic consensus motif (Fig. S2) retain the ability to bind chitin (26)(27)(28)(29)(30)(31)(32). Ala substitutions of conserved residues in the C-terminal domain of HmsF, the Yersinia pestis homolog of PgaB, had no effect on biofilm formation (33), further supporting the idea that PgaB 310-672 may be acting as a carbohydrate binding domain.…”

Section: Discussionmentioning

confidence: 99%

Modification and periplasmic translocation of the biofilm exopolysaccharide poly-β-1,6- N -acetyl- d -glucosamine

Little

Ing

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Poly-β-1,6-N-acetyl-D-glucosamine (PNAG) is an exopolysaccharide produced by a wide variety of medically important bacteria. Polyglucosamine subunit B (PgaB) is responsible for the de-N-acetylation of PNAG, a process required for polymer export and biofilm formation. PgaB is located in the periplasm and likely bridges the inner membrane synthesis and outer membrane export machinery. Here, we present structural, functional, and molecular simulation data that suggest PgaB associates with PNAG continuously during periplasmic transport. We show that the association of PgaB's N-and C-terminal domains forms a cleft required for the binding and de-N-acetylation of PNAG. Molecular dynamics (MD) simulations of PgaB show a binding preference for N-acetylglucosamine (GlcNAc) to the N-terminal domain and glucosammonium to the C-terminal domain. Continuous ligand binding density is observed that extends around PgaB from the N-terminal domain active site to an electronegative groove on the C-terminal domain that would allow for a processive mechanism. PgaB's C-terminal domain (PgaB 310-672 ) directly binds PNAG oligomers with dissociation constants of ∼1-3 mM, and the structures of PgaB 310-672 in complex with β-1,6-(GlcNAc) 6 , GlcNAc, and glucosamine reveal a unique binding mode suitable for interaction with de-N-acetylated PNAG (dPNAG). Furthermore, PgaB 310-672 contains a β-hairpin loop (βHL) important for binding PNAG that was disordered in previous PgaB 42-655 structures and is highly dynamic in the MD simulations. We propose that conformational changes in PgaB 310-672 mediated by the βHL on binding of PNAG/dPNAG play an important role in the targeting of the polymer for export and its release.exopolysaccharide biosynthesis | glycobiology | carbohydrate binding | deacetylase

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“…Likewise, the occurrence of GP40 seems restricted to artiodactyls. GP40 has been found to be present in dry mammary secretions at times when extensive tissue remodeling occurs (Srivastava et al 2006); hence its presence may reflect differences in mammary function between artiodactyls and other mammals.…”

Section: Discussionmentioning

confidence: 99%

Evolution of Mammalian Chitinase(-Like) Members of Family 18 Glycosyl Hydrolases

et al. 2007

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Family 18 of glycosyl hydrolases encompasses chitinases and so-called chi-lectins lacking enzymatic activity due to amino acid substitutions in their active site. Both types of proteins widely occur in mammals although these organisms lack endogenous chitin. Their physiological function(s) as well as evolutionary relationships are still largely enigmatic. An overview of all family members is presented and their relationships are described. Molecular phylogenetic analyses suggest that both active chitinases (chitotriosidase and AMCase) result from an early gene duplication event. Further duplication events, followed by mutations leading to loss of chitinase activity, allowed evolution of the chi-lectins. The homologous genes encoding chitinase(-like) proteins are clustered in two distinct loci that display a high degree of synteny among mammals. Despite the shared chromosomal location and high homology, individual genes have evolved independently. Orthologs are more closely related than paralogues, and calculated substitution rate ratios indicate that protein-coding sequences underwent purifying selection. Substantial gene specialization has occurred in time, allowing for tissue-specific expression of pH optimized chitinases and chilectins. Finally, several family 18 chitinase-like proteins are present only in certain lineages of mammals, exemplifying recent evolutionary events in the chitinase protein family.

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Crystal structure of a secretory signalling glycoprotein from sheep at 2.0 Å resolution

Cited by 24 publications

References 33 publications

Acute milk yield response to frequent milking during early lactation is mediated by genes transiently regulated by milk removal

Acute milk yield response to frequent milking during early lactation is mediated by genes transiently regulated by milk removal

Modification and periplasmic translocation of the biofilm exopolysaccharide poly-β-1,6- N -acetyl- d -glucosamine

Evolution of Mammalian Chitinase(-Like) Members of Family 18 Glycosyl Hydrolases

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