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The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase

Simpson, PJ; Jamieson, SJ; Abou-Hachem, Maher LU ; Nordberg Karlsson, Eva LU ; Gilbert, HJ; Holst, Olle LU and Williamson, MP (2002) In Biochemistry 41(18). p.5712-5719
Abstract
The solution structure is presented for the second family 4 carbohydrate binding module (CBM4-2) of xylanase 10A from the thermophilic bacterium Rhodothermus marinus. CBM4-2, which binds xylan tightly, has a beta-sandwich structure formed by I I strands, and contains a prominent cleft. From NMR titrations, it is shown that the cleft is the binding site for xylan, and that the main amino acids interacting with xylan are Asn31, Tyr69, Glu72, Phe110, Arg115, and His146. Key liganding residues are Tyr69 and Phe110, which form stacking interactions with the sugar. It is suggested that file loops Oil which the rings are displayed can alter their conformation on substrate binding, which may have functional importance. Comparison both with other... (More)
The solution structure is presented for the second family 4 carbohydrate binding module (CBM4-2) of xylanase 10A from the thermophilic bacterium Rhodothermus marinus. CBM4-2, which binds xylan tightly, has a beta-sandwich structure formed by I I strands, and contains a prominent cleft. From NMR titrations, it is shown that the cleft is the binding site for xylan, and that the main amino acids interacting with xylan are Asn31, Tyr69, Glu72, Phe110, Arg115, and His146. Key liganding residues are Tyr69 and Phe110, which form stacking interactions with the sugar. It is suggested that file loops Oil which the rings are displayed can alter their conformation on substrate binding, which may have functional importance. Comparison both with other family 4 cellulose binding modules and with the structurally similar family 22 xylan binding module shows that the key aromatic residues are in similar positions, and that the bottom of the cleft is much more hydrophobic in the cellulose binding module,, than the xylan binding proteins. It is concluded that substrate specificity is determined by a combination of ring Orientation and the nature of the residues lining the bottom of the binding cleft. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
41
issue
18
pages
5712 - 5719
publisher
The American Chemical Society
external identifiers
  • pmid:11980475
  • wos:000175365300003
  • scopus:0037035533
ISSN
0006-2960
DOI
10.1021/bi012093i
language
English
LU publication?
yes
id
dceb0d9e-c0d9-4d27-bca6-28d6d7d03593 (old id 338705)
date added to LUP
2007-11-13 15:49:02
date last changed
2017-09-03 03:46:40
@article{dceb0d9e-c0d9-4d27-bca6-28d6d7d03593,
  abstract     = {The solution structure is presented for the second family 4 carbohydrate binding module (CBM4-2) of xylanase 10A from the thermophilic bacterium Rhodothermus marinus. CBM4-2, which binds xylan tightly, has a beta-sandwich structure formed by I I strands, and contains a prominent cleft. From NMR titrations, it is shown that the cleft is the binding site for xylan, and that the main amino acids interacting with xylan are Asn31, Tyr69, Glu72, Phe110, Arg115, and His146. Key liganding residues are Tyr69 and Phe110, which form stacking interactions with the sugar. It is suggested that file loops Oil which the rings are displayed can alter their conformation on substrate binding, which may have functional importance. Comparison both with other family 4 cellulose binding modules and with the structurally similar family 22 xylan binding module shows that the key aromatic residues are in similar positions, and that the bottom of the cleft is much more hydrophobic in the cellulose binding module,, than the xylan binding proteins. It is concluded that substrate specificity is determined by a combination of ring Orientation and the nature of the residues lining the bottom of the binding cleft.},
  author       = {Simpson, PJ and Jamieson, SJ and Abou-Hachem, Maher and Nordberg Karlsson, Eva and Gilbert, HJ and Holst, Olle and Williamson, MP},
  issn         = {0006-2960},
  language     = {eng},
  number       = {18},
  pages        = {5712--5719},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase},
  url          = {http://dx.doi.org/10.1021/bi012093i},
  volume       = {41},
  year         = {2002},
}