1gny
From Proteopedia
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| - | [[Image:1gny. | + | [[Image:1gny.jpg|left|200px]]<br /><applet load="1gny" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gny" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1gny, resolution 1.63Å" /> | caption="1gny, resolution 1.63Å" /> | ||
'''XYLAN-BINDING MODULE CBM15'''<br /> | '''XYLAN-BINDING MODULE CBM15'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GNY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] | + | 1GNY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Site: <scene name='pdbsite=AC1:Xyp Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GNY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylooligosaccharide]] | [[Category: xylooligosaccharide]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:27:22 2007'' |
Revision as of 13:17, 18 December 2007
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XYLAN-BINDING MODULE CBM15
Overview
The recycling of photosynthetically fixed carbon by the action of, microbial glycoside hydrolases is a key biological process. The consortium, of degradative enzymes involved in this process frequently display, catalytic modules appended to one or more noncatalytic, carbohydrate-binding modules (CBMs). CBMs play a central role in the, optimization of the catalytic activity of plant cell wall hydrolases, through their binding to specific plant structural polysaccharides., Despite their pivotal role in the biodegradation of plant biomass, the, mechanism by which these proteins recognize their target ligands is, unclear. This report describes the structure of a xylan-binding CBM, (CBM15) in complex with its ligand. This module, derived from Pseudomonas, cellulosa xylanase Xyn10C, binds to both soluble xylan and, xylooligosaccharides. The three-dimensional crystal structure of CBM15, bound to xylopentaose has been solved by x-ray crystallography to a, resolution of 1.6 A. The protein displays a similar beta-jelly roll fold, to that observed in many other families of binding-modules. A groove, 20-25 A in length, on the concave surface of one of the beta-sheets, presents two tryptophan residues, the faces of which are orientated at, approximately 240 degrees to one another. These form-stacking interactions, with the n and n+2 sugars of xylopentaose complementing the approximate, 3-fold helical structure of this ligand in the binding cleft of CBM15. In, four of the five observed binding subsites, the 2' and 3' hydroxyls of the, bound ligand are solvent-exposed, providing an explanation for the, capacity of this xylan-binding CBM to accommodate the highly decorated, xylans found in the plant cell wall.
About this Structure
1GNY is a Single protein structure of sequence from Cellvibrio japonicus with NA as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation., Szabo L, Jamal S, Xie H, Charnock SJ, Bolam DN, Gilbert HJ, Davies GJ, J Biol Chem. 2001 Dec 28;276(52):49061-5. Epub 2001 Oct 11. PMID:11598143
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