2c24: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2c24.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2c24", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2c24|  PDB=2c24  |  SCENE=  }}
'''FAMILY 30 CARBOHYDRATE-BINDING MODULE OF CELLULOSOMAL CELLULASE CEL9D-CEL44B OF CLOSTRIDIUM THERMOCELLUM'''


==FAMILY 30 CARBOHYDRATE-BINDING MODULE OF CELLULOSOMAL CELLULASE CEL9D- CEL44B OF CLOSTRIDIUM THERMOCELLUM==
<StructureSection load='2c24' size='340' side='right'caption='[[2c24]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2c24]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C24 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c24 OCA], [https://pdbe.org/2c24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c24 RCSB], [https://www.ebi.ac.uk/pdbsum/2c24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c24 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P71140_ACETH P71140_ACETH]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzyme systems that attack the plant cell wall contain noncatalytic carbohydrate-binding modules (CBMs) that mediate attachment to this composite structure and play a pivotal role in maximizing the hydrolytic process. Although xyloglucan, which includes a backbone of beta-1,4-glucan decorated primarily with xylose residues, is a key component of the plant cell wall, CBMs that bind to this polymer have not been identified. Here we showed that the C-terminal domain of the modular Clostridium thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a novel CBM (designated CBM44) that binds with equal affinity to cellulose and xyloglucan. We also showed that accommodation of xyloglucan side chains is a general feature of CBMs that bind to single cellulose chains. The crystal structures of CBM44 and the other CBM (CBM30) in CtCel9D-Cel44A display a beta-sandwich fold. The concave face of both CBMs contains a hydrophobic platform comprising three tryptophan residues that can accommodate up to five glucose residues. The orientation of these aromatic residues is such that the bound ligand would adopt the twisted conformation displayed by cello-oligosaccharides in solution. Mutagenesis studies confirmed that the hydrophobic platform located on the concave face of both CBMs mediates ligand recognition. In contrast to other CBMs that bind to single polysaccharide chains, the polar residues in the binding cleft of CBM44 play only a minor role in ligand recognition. The mechanism by which these proteins are able to recognize linear and decorated beta-1,4-glucans is discussed based on the structures of CBM44 and the other CBMs that bind single cellulose chains.


==Overview==
Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains.,Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:16314409<ref>PMID:16314409</ref>
Enzyme systems that attack the plant cell wall contain noncatalytic carbohydrate-binding modules (CBMs) that mediate attachment to this composite structure and play a pivotal role in maximizing the hydrolytic process. Although xyloglucan, which includes a backbone of beta-1,4-glucan decorated primarily with xylose residues, is a key component of the plant cell wall, CBMs that bind to this polymer have not been identified. Here we showed that the C-terminal domain of the modular Clostridium thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a novel CBM (designated CBM44) that binds with equal affinity to cellulose and xyloglucan. We also showed that accommodation of xyloglucan side chains is a general feature of CBMs that bind to single cellulose chains. The crystal structures of CBM44 and the other CBM (CBM30) in CtCel9D-Cel44A display a beta-sandwich fold. The concave face of both CBMs contains a hydrophobic platform comprising three tryptophan residues that can accommodate up to five glucose residues. The orientation of these aromatic residues is such that the bound ligand would adopt the twisted conformation displayed by cello-oligosaccharides in solution. Mutagenesis studies confirmed that the hydrophobic platform located on the concave face of both CBMs mediates ligand recognition. In contrast to other CBMs that bind to single polysaccharide chains, the polar residues in the binding cleft of CBM44 play only a minor role in ligand recognition. The mechanism by which these proteins are able to recognize linear and decorated beta-1,4-glucans is discussed based on the structures of CBM44 and the other CBMs that bind single cellulose chains.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2C24 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C24 OCA].
</div>
<div class="pdbe-citations 2c24" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains., Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM, J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16314409 16314409]
*[[Glucanase 3D structures|Glucanase 3D structures]]
[[Category: Clostridium thermocellum]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Alves, V.]]
__TOC__
[[Category: Bolam, D N.]]
</StructureSection>
[[Category: Carvalho, A L.]]
[[Category: Acetivibrio thermocellus]]
[[Category: Ferreira, L M.A.]]
[[Category: Large Structures]]
[[Category: Fontes, C M.G A.]]
[[Category: Alves VD]]
[[Category: Gilbert, H J.]]
[[Category: Bolam DN]]
[[Category: Najmudin, S.]]
[[Category: Carvalho AL]]
[[Category: Prates, J A.M.]]
[[Category: Ferreira LMA]]
[[Category: Romao, M J.]]
[[Category: Fontes CMGA]]
[[Category: Cbm30]]
[[Category: Gilbert HJ]]
[[Category: Cellulosome]]
[[Category: Najmudin S]]
[[Category: Clostridium thermocellum]]
[[Category: Prates JAM]]
[[Category: Hydrolase]]
[[Category: Romao MJ]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:07:49 2008''

Latest revision as of 10:24, 6 September 2023

FAMILY 30 CARBOHYDRATE-BINDING MODULE OF CELLULOSOMAL CELLULASE CEL9D- CEL44B OF CLOSTRIDIUM THERMOCELLUM

2c24, resolution 2.27Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2c24&oldid=3870334"