2XQO

CtCel124: a cellulase from Clostridium thermocellum

Summary for 2XQO

• Entry DOI: 10.2210/pdb2xqo/pdb
• Related PRD ID: PRD_900021
• Descriptor: Dockerin type 1, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
• Total number of polymer chains: 1
• Total formula weight: 29013.20

Authors

Carvalho, A.L.,Verze, G.,Bras, J.L.A.,Cartmell, A.,Bayer, E.A.,Vazana, Y.,Correia, M.A.S.,Prates, J.A.M.,Gilbert, H.J.,Fontes, C.M.G.A.,Romao, M.J. (deposition date: 2010-09-06, release date: 2011-03-02, Last modification date: 2024-10-16)

Primary citation

Bras, J.L.A.,Cartmell, A.,Carvalho, A.L.,Verze, G.,Bayer, E.A.,Vazana, Y.,Correia, M.A.S.,Prates, J.A.M.,Romao, M.J.,Gilbert, H.J.,Fontes, C.M.G.A.
Structural Insights Into a Unique Cellulase Fold and Mechanism of Cellulose Hydrolysis
Proc.Natl.Acad.Sci.USA, 108:5237-, 2011

PubMed Abstract: Clostridium thermocellum is a well-characterized cellulose-degrading microorganism. The genome sequence of C. thermocellum encodes a number of proteins that contain type I dockerin domains, which implies that they are components of the cellulose-degrading apparatus, but display no significant sequence similarity to known plant cell wall-degrading enzymes. Here, we report the biochemical properties and crystal structure of one of these proteins, designated CtCel124. The protein was shown to be an endo-acting cellulase that displays a single displacement mechanism and acts in synergy with Cel48S, the major cellulosomal exo-cellulase. The crystal structure of CtCel124 in complex with two cellotriose molecules, determined to 1.5 Å, displays a superhelical fold in which a constellation of α-helices encircle a central helix that houses the catalytic apparatus. The catalytic acid, Glu96, is located at the C-terminus of the central helix, but there is no candidate catalytic base. The substrate-binding cleft can be divided into two discrete topographical domains in which the bound cellotriose molecules display twisted and linear conformations, respectively, suggesting that the enzyme may target the interface between crystalline and disordered regions of cellulose.

PubMed: 21393568
DOI: 10.1073/PNAS.1015006108

Experimental method

X-RAY DIFFRACTION (1.4 Å)