2bvd

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|PDB= 2bvd |SIZE=350|CAPTION= <scene name='initialview01'>2bvd</scene>, resolution 1.60&Aring;
|PDB= 2bvd |SIZE=350|CAPTION= <scene name='initialview01'>2bvd</scene>, resolution 1.60&Aring;
|SITE= <scene name='pdbsite=AC1:Isx+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Isx+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ISX:GLUCOSE BETA-1,3-ISOFAGAMINE'>ISX</scene>
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|LIGAND= <scene name='pdbligand=ISX:GLUCOSE+BETA-1,3-ISOFAGAMINE'>ISX</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bvd OCA], [http://www.ebi.ac.uk/pdbsum/2bvd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bvd RCSB]</span>
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}}
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[[Category: Stick, R V.]]
[[Category: Stick, R V.]]
[[Category: Taylor, E J.]]
[[Category: Taylor, E J.]]
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[[Category: ISX]]
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[[Category: lichenase,beta-1 4 beta-1 3 glucanase,glycoside hydrolase family 26]]
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[[Category: beta-1 4 beta-1 3 glucanase]]
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[[Category: glycoside hydrolase family 26]]
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[[Category: lichenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:07:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:12:18 2008''

Revision as of 23:12, 30 March 2008


PDB ID 2bvd

Drag the structure with the mouse to rotate
, resolution 1.60Å
Sites:
Ligands:
Activity: Cellulase, with EC number 3.2.1.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CTLIC26A


Overview

One of the most intriguing features of the 90 glycoside hydrolase families (GHs) is the range of specificities displayed by different members of the same family, whereas the catalytic apparatus and mechanism are often invariant. Family GH26 predominantly comprises beta-1,4 mannanases; however, a bifunctional Clostridium thermocellum GH26 member (hereafter CtLic26A) displays a markedly different specificity. We show that CtLic26A is a lichenase, specific for mixed (Glcbeta1,4Glcbeta1,4Glcbeta1,3)n oligo- and polysaccharides, and displays no activity on manno-configured substrates or beta-1,4-linked homopolymers of glucose or xylose. The three-dimensional structure of the native form of CtLic26A has been solved at 1.50-A resolution, revealing a characteristic (beta/alpha)8 barrel with Glu-109 and Glu-222 acting as the catalytic acid/base and nucleophile in a double-displacement mechanism. The complex with the competitive inhibitor, Glc-beta-1,3-isofagomine (Ki 1 microm), at 1.60 A sheds light on substrate recognition in the -2 and -1 subsites and illuminates why the enzyme is specific for lichenan-based substrates. Hydrolysis of beta-mannosides by GH26 members is thought to proceed through transition states in the B2,5 (boat) conformation in which structural distinction of glucosides versus mannosides reflects not the configuration at C2 but the recognition of the pseudoaxial O3 of the B2,5 conformation. We suggest a different conformational itinerary for the GH26 enzymes active on gluco-configured substrates.

About this Structure

2BVD is a Single protein structure of sequence from Clostridium thermocellum. Full crystallographic information is available from OCA.

Reference

How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A., Taylor EJ, Goyal A, Guerreiro CI, Prates JA, Money VA, Ferry N, Morland C, Planas A, Macdonald JA, Stick RV, Gilbert HJ, Fontes CM, Davies GJ, J Biol Chem. 2005 Sep 23;280(38):32761-7. Epub 2005 Jun 28. PMID:15987675

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