PDBsum entry: 2w87

Hydrolase

PDB-id: 2w87

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Description

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References

PROCHECK

Protein chains

139 a.a. *

Ligands

GCU-UNL ×2

Metal ions

_CA ×4

Waters ×304

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

2w87

Name:

Hydrolase

Title:

Xyl-cbm35 in complex with glucuronic acid containing disaccharide.

Structure:

Esterase d. Chain: a, b. Fragment: residues 160-298. Synonym: xyl-cbm35. Engineered: yes

Source:

Cellvibrio japonicus. Organism_taxid: 155077. Expressed in: escherichia coli. Expression_system_taxid: 469008.

UniProt:

Chains A, B: Q51815 (Q51815_9GAMM)

Seq:

Struc:

Seq:

Struc:

Seq:

583 a.a.

Struc:

139 a.a.

Key:

PfamA domain

Secondary structure

Resolution:

1.60Å

R-factor:

0.145

R-free:

0.193

Authors:

C.Montainer,A.L.V.Bueren,C.Dumon,J.E.Flint,M.A.Correia, J.A.Prates,S.J.Firbank,R.J.Lewis,G.G.Grondin,M.G.Ghinet, T.M.Gloster,C.Herve,J.P.Knox,B.G.Talbot,J.P.Turkenburg, J.Kerovuo,R.Brzezinski,C.M.G.A.Fontes,G.J.Davies, A.B.Boraston,H.J.Gilbert

Key ref:

C.Montanier et al. (2009). Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.. Proc Natl Acad Sci U S A, 106, 3065-3070. [PubMed id: 19218457]

Date:

14-Jan-09

Release date:

27-Jan-09

Related entries:

2w46 cbm35 from cellvibrio japonicus abf62

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Procheck

Clefts

Surface

Key reference

Proc Natl Acad Sci U S A 106:3065-3070 (2009)

PubMed id: 19218457

Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.

C.Montanier, A.L.van Bueren, C.Dumon, J.E.Flint, M.A.Correia, J.A.Prates, S.J.Firbank, R.J.Lewis, G.G.Grondin, M.G.Ghinet, T.M.Gloster, C.Herve, J.P.Knox, B.G.Talbot, J.P.Turkenburg, J.Kerovuo, R.Brzezinski, C.M.Fontes, G.J.Davies, A.B.Boraston, H.J.Gilbert.

ABSTRACT

Enzymes that hydrolyze complex carbohydrates play important roles in numerous biological processes that result in the maintenance of marine and terrestrial life. These enzymes often contain noncatalytic carbohydrate binding modules (CBMs) that have important substrate-targeting functions. In general, there is a tight correlation between the ligands recognized by bacterial CBMs and the substrate specificity of the appended catalytic modules. Through high-resolution structural studies, we demonstrate that the architecture of the ligand binding sites of 4 distinct family 35 CBMs (CBM35s), appended to 3 plant cell wall hydrolases and the exo-beta-D-glucosaminidase CsxA, which contributes to the detoxification and metabolism of an antibacterial fungal polysaccharide, is highly conserved and imparts specificity for glucuronic acid and/or Delta4,5-anhydrogalaturonic acid (Delta4,5-GalA). Delta4,5-GalA is released from pectin by the action of pectate lyases and as such acts as a signature molecule for plant cell wall degradation. Thus, the CBM35s appended to the 3 plant cell wall hydrolases, rather than targeting the substrates of the cognate catalytic modules, direct their appended enzymes to regions of the plant that are being actively degraded. Significantly, the CBM35 component of CsxA anchors the enzyme to the bacterial cell wall via its capacity to bind uronic acid sugars. This latter observation reveals an unusual mechanism for bacterial cell wall enzyme attachment. This report shows that the biological role of CBM35s is not dictated solely by their carbohydrate specificities but also by the context of their target ligands.