PDBsum entry: 1gui

Carbohydrate binding module

PDB-id

1gui


	Biological unit = asymmetric unit, as shown (as defined in PDB file)

Contents

Description

Header details

Protein chain

Ligands

GOL ×5

BGC-BGC-BGC-BGC-
BGC-BGC

Metal ions

_CA

Waters ×111

* Residue conservation analysis

Tools

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PDB id:

1gui

Name:

Carbohydrate binding module

Title:

Cbm4 structure and function

Structure:

Laminarinase 16a. Chain: a. Fragment: residues 488-642. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 511693. Other_details: carbohydrate binding module of laminarinase 16a from thermotoga maritima

Biological unit:

Monomer (from PDB file)

UniProt:

Q9WXN1 (Q9WXN1_THEMA)

Seq:

Struc:

Seq:

Struc:

Seq:

642 a.a.

Struc:

155 a.a.*

Key:		PfamA domain
		Secondary structure			CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

Resolution:

1.9Å

R-factor:

0.173

R-free:

0.197

Authors:

D.Nurizzo,V.Notenboom,G.J.Davies

Key ref:

A.B.Boraston et al. (2002). Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules.. J Mol Biol, 319, 1143-1156. [PubMed id: 12079353] [DOI: 10.1016/S0022-2836(02)00374-1]

Date:

27-Jan-02

Release date:

26-Sep-02

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Key reference

DOI no: 10.1016/S0022-2836(02)00374-1 J Mol Biol 319:1143-1156 (2002)

PubMed id: 12079353

Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules.

A.B.Boraston, D.Nurizzo, V.Notenboom, V.Ducros, D.R.Rose, D.G.Kilburn, G.J.Davies.

ABSTRACT

Enzymes active on complex carbohydrate polymers frequently have modular structures in which a catalytic domain is appended to one or more carbohydrate-binding modules (CBMs). Although CBMs have been classified into a number of families based upon sequence, many closely related CBMs are specific for different polysaccharides. In order to provide a structural rationale for the recognition of different polysaccharides by CBMs displaying a conserved fold, we have studied the thermodynamics of binding and three-dimensional structures of the related family 4 CBMs from Cellulomonas fimi Cel9B and Thermotoga maritima Lam16A in complex with their ligands, beta-1,4 and beta-1,3 linked gluco-oligosaccharides, respectively. These two CBMs use a structurally conserved constellation of aromatic and polar amino acid side-chains that interact with sugars in two of the five binding subsites. Differences in the length and conformation of loops in non-conserved regions create binding-site topographies that complement the known solution conformations of their respective ligands. Thermodynamics interpreted in the light of structural information highlights the differential role of water in the interaction of these CBMs with their respective oligosaccharide ligands.

Selected figure(s)

Figure 3.
Figure 3. Overlap of the observed oligosaccharide conformations for the b-1,4 and b-1,3 glucan chains on (a) CfCBM4-1 and (b) TmCBM4-2 (b;ue) with the solution conformations for these ligands (green).[31. and 37.] Only the five sugar units of laminarihexoase making interactions with TmCBM4-2 are shown. Figure 4.
Figure 4. A schematic showing (a) the CfCBM4-1-cellopentaose interactions and (b) TmCBM4-2-laminariheptaose interactions. Sugar units that are structurally-equivalent are shown in red and blue.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 319, 1143-1156) copyright 2002.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id Reference

19257855 E.A.Chavelas, and E.García-Hernández (2009).
Heat capacity changes in carbohydrates and protein-carbohydrate complexes.

Biochem J, 420, 239-247.

19116695 R.E.Nordon, S.J.Craig, and F.C.Foong (2009).
Molecular engineering of the cellulosome complex for affinity and bioenergy applications.

Biotechnol Lett, 31, 465-476.

18802694 Y.M.Cheng, T.Y.Hong, C.C.Liu, and M.Meng (2009).
Cloning and functional characterization of a complex endo-beta-1,3-glucanase from Paenibacillus sp.

Appl Microbiol Biotechnol, 81, 1051-1061.

18422658 A.Viegas, N.F.Brás, N.M.Cerqueira, P.A.Fernandes, J.A.Prates, C.M.Fontes, M.Bruix, M.J.Romão, A.L.Carvalho, M.J.Ramos, A.L.Macedo, and E.J.Cabrita (2008).
Molecular determinants of ligand specificity in family 11 carbohydrate binding modules: an NMR, X-ray crystallography and computational chemistry approach.

FEBS J, 275, 2524-2535.

18025086 B.Bae, S.Ohene-Adjei, S.Kocherginskaya, R.I.Mackie, M.A.Spies, I.K.Cann, and S.K.Nair (2008).
Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA.

J Biol Chem, 283, 12415-12425.

PDB codes: 2zew 2zex 2zey 2zez

18292090 K.J.Gregg, R.Finn, D.W.Abbott, and A.B.Boraston (2008).
Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.

J Biol Chem, 283, 12604-12613.

PDB codes: 2vmg 2vmh 2vmi 2vng 2vno 2vnr

18663584 L.C.Tsai, Y.N.Chen, and L.F.Shyur (2008).
Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-D-glucanases.

J Comput Aided Mol Des, 22, 915-923.

18784084 M.E.Caines, H.Zhu, M.Vuckovic, L.M.Willis, S.G.Withers, W.W.Wakarchuk, and N.C.Strynadka (2008).
The Structural Basis for T-antigen Hydrolysis by Streptococcus pneumoniae: A TARGET FOR STRUCTURE-BASED VACCINE DESIGN.

J Biol Chem, 283, 31279-31283.

PDB code: 3ecq

17554045 C.R.Pigott, and D.J.Ellar (2007).
Role of receptors in Bacillus thuringiensis crystal toxin activity.

Microbiol Mol Biol Rev, 71, 255-281.

17690769 E.C.Stanca-Kaposta, D.P.Gamblin, J.Screen, B.Liu, L.C.Snoek, B.G.Davis, and J.P.Simons (2007).
Carbohydrate molecular recognition: a spectroscopic investigation of carbohydrate-aromatic interactions.

Phys Chem Chem Phys, 9, 4444-4451.

16230347 A.B.Boraston, M.Healey, J.Klassen, E.Ficko-Blean, A.Lammerts van Bueren, and V.Law (2006).
A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition.

J Biol Chem, 281, 587-598.

PDB codes: 2c3g 2c3h 2c3v 2c3w 2c3x

16456543 A.R.Aricescu, W.C.Hon, C.Siebold, W.Lu, P.A.van der Merwe, and E.Y.Jones (2006).
Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion.

EMBO J, 25, 701-712.

PDB code: 2c9a

16844685 A.W.Blake, L.McCartney, J.E.Flint, D.N.Bolam, A.B.Boraston, H.J.Gilbert, and J.P.Knox (2006).
Understanding the biological rationale for the diversity of cellulose-directed carbohydrate-binding modules in prokaryotic enzymes.

J Biol Chem, 281, 29321-29329.

16601125 J.Henshaw, A.Horne-Bitschy, A.L.van Bueren, V.A.Money, D.N.Bolam, M.Czjzek, N.A.Ekborg, R.M.Weiner, S.W.Hutcheson, G.J.Davies, A.B.Boraston, and H.J.Gilbert (2006).
Family 6 carbohydrate binding modules in beta-agarases display exquisite selectivity for the non-reducing termini of agarose chains.

J Biol Chem, 281, 17099-17107.

PDB codes: 2cdo 2cdp

16537424 L.McCartney, A.W.Blake, J.Flint, D.N.Bolam, A.B.Boraston, H.J.Gilbert, and J.P.Knox (2006).
Differential recognition of plant cell walls by microbial xylan-specific carbohydrate-binding modules.

Proc Natl Acad Sci U S A, 103, 4765-4770.

17005007 M.S.Centeno, A.Goyal, J.A.Prates, L.M.Ferreira, H.J.Gilbert, and C.M.Fontes (2006).
Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus.

FEMS Microbiol Lett, 265, 26-34.

15501830 A.L.van Bueren, C.Morland, H.J.Gilbert, and A.B.Boraston (2005).
Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface.

J Biol Chem, 280, 530-537.

PDB codes: 1w9s 1w9t 1w9w

15784618 J.Flint, D.N.Bolam, D.Nurizzo, E.J.Taylor, M.P.Williamson, C.Walters, G.J.Davies, and H.J.Gilbert (2005).
Probing the mechanism of ligand recognition in family 29 carbohydrate-binding modules.

J Biol Chem, 280, 23718-23726.

PDB codes: 1w8t 1w8u 1w8w 1w8z 1w90 1w9f 1wcu

15192099 A.L.Carvalho, A.Goyal, J.A.Prates, D.N.Bolam, H.J.Gilbert, V.M.Pires, L.M.Ferreira, A.Planas, M.J.Romão, and C.M.Fontes (2004).
The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site.

J Biol Chem, 279, 34785-34793.

PDB code: 1v0a

15004012 D.N.Bolam, H.Xie, G.Pell, D.Hogg, G.Galbraith, B.Henrissat, and H.J.Gilbert (2004).
X4 modules represent a new family of carbohydrate-binding modules that display novel properties.

J Biol Chem, 279, 22953-22963.

15004011 J.L.Henshaw, D.N.Bolam, V.M.Pires, M.Czjzek, B.Henrissat, L.M.Ferreira, C.M.Fontes, and H.J.Gilbert (2004).
The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities.

J Biol Chem, 279, 21552-21559.

15010454 V.M.Pires, J.L.Henshaw, J.A.Prates, D.N.Bolam, L.M.Ferreira, C.M.Fontes, B.Henrissat, A.Planas, H.J.Gilbert, and M.Czjzek (2004).
The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities.

J Biol Chem, 279, 21560-21568.

PDB codes: 1uxx 1uxz 1uy0 1uyx 1uyy 1uyz 1uz0

12427734 A.B.Boraston, E.Kwan, P.Chiu, R.A.Warren, and D.G.Kilburn (2003).
Recognition and hydrolysis of noncrystalline cellulose.

J Biol Chem, 278, 6120-6127.

12391332 S.J.Charnock, D.N.Bolam, D.Nurizzo, L.Szabó, V.A.McKie, H.J.Gilbert, and G.J.Davies (2002).
Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose.

Proc Natl Acad Sci U S A, 99, 14077-14082.

PDB codes: 1gwk 1gwl 1gwm

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.