1gmm
From Proteopedia
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| - | [[Image:1gmm.gif|left|200px]]<br /><applet load="1gmm" size=" | + | [[Image:1gmm.gif|left|200px]]<br /><applet load="1gmm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gmm, resolution 2.0Å" /> | caption="1gmm, resolution 2.0Å" /> | ||
'''CARBOHYDRATE BINDING MODULE CBM6 FROM XYLANASE U CLOSTRIDIUM THERMOCELLUM'''<br /> | '''CARBOHYDRATE BINDING MODULE CBM6 FROM XYLANASE U CLOSTRIDIUM THERMOCELLUM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with SO4, NA and CA as [http://en.wikipedia.org/wiki/ligands ligands]. 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=CA1:Ca Binding Site For Chain A'>CA1</scene>. Full crystallographic information is available from [http:// | + | 1GMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=CA1:Ca+Binding+Site+For+Chain+A'>CA1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylan binding]] | [[Category: xylan binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:41:03 2008'' |
Revision as of 07:41, 3 February 2008
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CARBOHYDRATE BINDING MODULE CBM6 FROM XYLANASE U CLOSTRIDIUM THERMOCELLUM
Overview
Polysaccharide-degrading enzymes are generally modular proteins that, contain non-catalytic carbohydrate-binding modules (CBMs), which, potentiate the activity of the catalytic module. CBMs have been grouped, into sequence-based families, and three-dimensional structural data are, available for half of these families. Clostridium thermocellum xylanase, 11A is a modular enzyme that contains a CBM from family 6 (CBM6), for, which no structural data are available. We have determined the crystal, structure of this module to a resolution of 2.1 A. The protein is a, beta-sandwich that contains two potential ligand-binding clefts designated, cleft A and B. The CBM interacts primarily with xylan, and NMR, spectroscopy coupled with site-directed mutagenesis identified cleft A, containing Trp-92, Tyr-34, and Asn-120, as the ligand-binding site. The, overall fold of CBM6 is similar to proteins in CBM families 4 and 22, although surprisingly the ligand-binding site in CBM4 and CBM22 is, equivalent to cleft B in CBM6. These structural data define a superfamily, of CBMs, comprising CBM4, CBM6, and CBM22, and demonstrate that, although, CBMs have evolved from a relatively small number of ancestors, the, structural elements involved in ligand recognition have been assembled at, different locations on the ancestral scaffold.
About this Structure
1GMM is a Single protein structure of sequence from Clostridium thermocellum with , and as ligands. 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
The location of the ligand-binding site of carbohydrate-binding modules that have evolved from a common sequence is not conserved., Czjzek M, Bolam DN, Mosbah A, Allouch J, Fontes CM, Ferreira LM, Bornet O, Zamboni V, Darbon H, Smith NL, Black GW, Henrissat B, Gilbert HJ, J Biol Chem. 2001 Dec 21;276(51):48580-7. Epub 2001 Oct 22. PMID:11673472
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