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Polar interactions with branching xyloses and CH-π interactions define carbohydrate binding module recognition of xyloglucan

von Schantz, Laura LU ; Håkansson, Maria; Logan, Derek LU ; Nordberg Karlsson, Eva LU and Ohlin, Mats LU (2014) In Proteins 82(12). p.3466-3475
Abstract
Engineering of novel carbohydrate-binding proteins that can be utilized in various biochemical and biotechnical applications would benefit from a deeper understanding of the biochemical interactions that determine protein-carbohydrate specificity. In an effort to understand further the basis for specificity we present the crystal structure of the multi-specific carbohydrate-binding module (CBM) X-2 L110F bound to a branched oligomer of xyloglucan (XXXG). X-2 L110F is an engineered CBM that can recognize xyloglucan, xylans and β-glucans. The structural observations of the present study compared with previously reported structures of X-2 L110F in complex with linear oligomers, show that the π-surface of a phenylalanine, F110, allows for... (More)
Engineering of novel carbohydrate-binding proteins that can be utilized in various biochemical and biotechnical applications would benefit from a deeper understanding of the biochemical interactions that determine protein-carbohydrate specificity. In an effort to understand further the basis for specificity we present the crystal structure of the multi-specific carbohydrate-binding module (CBM) X-2 L110F bound to a branched oligomer of xyloglucan (XXXG). X-2 L110F is an engineered CBM that can recognize xyloglucan, xylans and β-glucans. The structural observations of the present study compared with previously reported structures of X-2 L110F in complex with linear oligomers, show that the π-surface of a phenylalanine, F110, allows for interactions with hydrogen atoms on both linear (xylopentaose and cellopentaose) and branched ligands (XXXG). Furthermore, X-2 L110F is shown to have a relatively flexible binding cleft, as illustrated in binding to XXXG. This branched ligand requires a set of reorientations of protein side chains Q72, N31, and R142, although these residues have previously been determined as important for binding to xylose oligomers by mediating polar contacts. The loss of these polar contacts is compensated for in binding to XXXG by polar interactions mediated by other protein residues, T74, R115, and Y149, which interact mainly with the branching xyloses of the xyloglucan oligomer. Taken together, the present study illustrates in structural detail how CH-π interactions can influence binding specificity and that flexibility is a key feature for the multi-specificity displayed by X-2 L110F, allowing for the accommodation of branched ligands. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Proteins
volume
82
issue
12
pages
3466 - 3475
publisher
John Wiley & Sons
external identifiers
  • pmid:25302425
  • wos:000345305400019
  • scopus:84937597400
ISSN
0887-3585
DOI
10.1002/prot.24700
language
English
LU publication?
yes
id
6b9557e7-5061-4e73-86a1-eb457ad4edd1 (old id 4762082)
date added to LUP
2014-11-06 14:48:17
date last changed
2017-09-03 03:02:35
@article{6b9557e7-5061-4e73-86a1-eb457ad4edd1,
  abstract     = {Engineering of novel carbohydrate-binding proteins that can be utilized in various biochemical and biotechnical applications would benefit from a deeper understanding of the biochemical interactions that determine protein-carbohydrate specificity. In an effort to understand further the basis for specificity we present the crystal structure of the multi-specific carbohydrate-binding module (CBM) X-2 L110F bound to a branched oligomer of xyloglucan (XXXG). X-2 L110F is an engineered CBM that can recognize xyloglucan, xylans and β-glucans. The structural observations of the present study compared with previously reported structures of X-2 L110F in complex with linear oligomers, show that the π-surface of a phenylalanine, F110, allows for interactions with hydrogen atoms on both linear (xylopentaose and cellopentaose) and branched ligands (XXXG). Furthermore, X-2 L110F is shown to have a relatively flexible binding cleft, as illustrated in binding to XXXG. This branched ligand requires a set of reorientations of protein side chains Q72, N31, and R142, although these residues have previously been determined as important for binding to xylose oligomers by mediating polar contacts. The loss of these polar contacts is compensated for in binding to XXXG by polar interactions mediated by other protein residues, T74, R115, and Y149, which interact mainly with the branching xyloses of the xyloglucan oligomer. Taken together, the present study illustrates in structural detail how CH-π interactions can influence binding specificity and that flexibility is a key feature for the multi-specificity displayed by X-2 L110F, allowing for the accommodation of branched ligands.},
  author       = {von Schantz, Laura and Håkansson, Maria and Logan, Derek and Nordberg Karlsson, Eva and Ohlin, Mats},
  issn         = {0887-3585},
  language     = {eng},
  number       = {12},
  pages        = {3466--3475},
  publisher    = {John Wiley & Sons},
  series       = {Proteins},
  title        = {Polar interactions with branching xyloses and CH-π interactions define carbohydrate binding module recognition of xyloglucan},
  url          = {http://dx.doi.org/10.1002/prot.24700},
  volume       = {82},
  year         = {2014},
}