PDBsum entry 1jw5

Sugar binding protein

PDB id

1jw5

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Contents

			Protein chain

					370 a.a. *

			Ligands

					GLC-GLC

			Waters ×301

* Residue conservation analysis

PDB id:

1jw5

Links

Name:

Sugar binding protein

Title:

Structure of maltose bound to open-form maltodextrin-binding protein in p1 crystal

Structure:

Maltodextrin-binding protein. Chain: a. Synonym: maltose-binding periplasmic protein. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å

R-factor:

0.195

R-free:

0.253

Authors:

X.Duan,F.A.Quiocho

Key ref:

X.Duan and F.A.Quiocho (2002). Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands. Biochemistry, 41, 706-712. PubMed id: 11790091 DOI: 10.1021/bi015784n

Date:

02-Sep-01

Release date:

30-Jan-02

PROCHECK

	Headers

	References

Protein chain

P0AEX9 (MALE_ECOLI) - Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)

Seq: Struc:					396 a.a. 370 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi015784n	Biochemistry 41:706-712 (2002)
PubMed id: 11790091

Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands.
X.Duan, F.A.Quiocho.

ABSTRACT

The receptor, a maltose/maltooligosaccharide-binding protein, has been found to be an excellent system for the study of molecular recognition because its polar and nonpolar binding functions are segregated into two globular domains. The X-ray structures of the "closed" and "open" forms of the protein complexed with maltose and maltotetraitol have been determined. These sugars have approximately 3 times more accessible polar surface (from OH groups) than nonpolar surface (from small clusters of sugar ring CH bonds). In the closed structures, the oligosaccharides are buried in the groove between the two domains of the protein and bound by extensive hydrogen bonding interactions of the OH groups with the polar residues confined mostly in one domain and by nonpolar interactions of the CH clusters with four aromatic residues lodged in the other domain. Substantial contacts between the sugar hydroxyls and aromatic residues are also formed. In the open structures, the oligosaccharides are bound almost exclusively in the domain rich in aromatic residues. This finding, along with the analysis of buried surface area due to complex formations in the open and closed structures, supports a major role for nonpolar interactions in initial ligand binding even when the ligands have significantly greater potential for highly specific polar interactions.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21420935

Y.Zhang, X.Gao, and R.Michael Garavito (2011).
Structural analysis of the intracellular domain of (pro)renin receptor fused to maltose-binding protein.

Biochem Biophys Res Commun, 407, 674-679.

PDB codes:

3lbs 3lc8

20535468

I.H.Walker, P.C.Hsieh, and P.D.Riggs (2010).
Mutations in maltose-binding protein that alter affinity and solubility properties.

Appl Microbiol Biotechnol, 88, 187-197.

19801540

M.J.Cuneo, L.S.Beese, and H.W.Hellinga (2009).
Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold.

J Biol Chem, 284, 33217-33223.

PDB codes:

2o7i 3i5o

18535149

A.L.Davidson, E.Dassa, C.Orelle, and J.Chen (2008).
Structure, function, and evolution of bacterial ATP-binding cassette systems.

Microbiol Mol Biol Rev, 72, 317.

18818359

B.W.Han, B.R.Herrin, M.D.Cooper, and I.A.Wilson (2008).
Antigen recognition by variable lymphocyte receptors.

Science, 321, 1834-1837.

PDB code:

3e6j

17960247

C.Tang, C.D.Schwieters, and G.M.Clore (2007).
Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR.

Nature, 449, 1078-1082.

PDB code:

2v93

18033289

M.L.Oldham, D.Khare, F.A.Quiocho, A.L.Davidson, and J.Chen (2007).
Crystal structure of a catalytic intermediate of the maltose transporter.

Nature, 450, 515-521.

PDB code:

2r6g

17242374

N.C.Vercillo, K.J.Herald, J.M.Fox, B.S.Der, and J.D.Dattelbaum (2007).
Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy.

Protein Sci, 16, 362-368.

15770624

A.Carvalho de Souza, K.M.Halkes, J.D.Meeldijk, A.J.Verkleij, J.F.Vliegenthart, and J.P.Kamerling (2005).
Gold glyconanoparticles as probes to explore the carbohydrate-mediated self-recognition of marine sponge cells.

Chembiochem, 6, 828-831.

16511036

N.V.Adikesavan, S.S.Mahmood, N.Stanley, Z.Xu, N.Wu, M.Thibonnier, and M.Shoham (2005).
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 341-345.

PDB code:

1ytv

16143635

T.Stockner, H.J.Vogel, and D.P.Tieleman (2005).
A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein.

Biophys J, 89, 3362-3371.

15281134

D.B.Sherman, S.Zhang, J.B.Pitner, and A.Tropsha (2004).
Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.

Proteins, 56, 828-838.

15304639

L.Guan, and H.R.Kaback (2004).
Binding affinity of lactose permease is not altered by the H+ electrochemical gradient.

Proc Natl Acad Sci U S A, 101, 12148-12152.

14527411

J.Chen, G.Lu, J.Lin, A.L.Davidson, and F.A.Quiocho (2003).
A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle.

Mol Cell, 12, 651-661.

PDB codes:

1q12 1q1b 1q1e

14530390

O.Millet, R.P.Hudson, and L.E.Kay (2003).
The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy.

Proc Natl Acad Sci U S A, 100, 12700-12705.

12925992

Q.Vicens, and E.Westhof (2003).
Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: an analysis of x-ray crystal structures.

Biopolymers, 70, 42-57.

11875510

W.E.Meador, and F.A.Quiocho (2002).
Man bites dog.

Nat Struct Biol, 9, 156-158.

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.