1F9D

Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellotetraose

Summary for 1F9D

• Entry DOI: 10.2210/pdb1f9d/pdb
• Related: 1F9O 1FAE 1FBO 1FBW 1FCE
• Related PRD ID: PRD_900010 PRD_900030
• Descriptor: ENDO-1,4-BETA-GLUCANASE F, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: cellulase, protein-cellotetraose complex, hydrolase
• Biological source: Clostridium cellulolyticum
• Total number of polymer chains: 1
• Total formula weight: 72404.27

Authors

Parsiegla, G.,Reverbel-Leroy, C.,Tardif, C.,Belaich, J.P.,Driguez, H.,Haser, R. (deposition date: 2000-07-10, release date: 2000-08-02, Last modification date: 2024-02-07)

Primary citation

Parsiegla, G.,Reverbel-Leroy, C.,Tardif, C.,Belaich, J.P.,Driguez, H.,Haser, R.
Crystal Structures of the Cellulase Cel48F in Complex with Inhibitors and Substrates Give Insights Into its Processive Action
Biochemistry, 39:11238-11246, 2000

PubMed Abstract: Cellulase Cel48F from Clostridium cellulolyticum was described as a processive endo-cellulase. The active site is composed of a 25 A long tunnel which is followed by an open cleft. During the processive action, the cellulose substrate has to slide through the tunnel to continuously supply the leaving group site with sugar residues after the catalytic cleavage. To study this processive action in the tunnel, the native catalytic module of Cel48F and the inactive mutant E55Q, have been cocrystallized with cellobiitol, two thio-oligosaccharide inhibitors (PIPS-IG3 and IG4) and the cello-oligosaccharides cellobiose, -tetraose and -hexaose. Seven sub-sites in the tunnel section of the active center could be identified and three of the four previously reported sub-sites in the open cleft section were reconfirmed. The sub-sites observed for the thio-oligosaccharide inhibitors and oligosaccharides, respectively, were located at two different positions in the tunnel corresponding to a shift in the chain direction of about a half sugar subunit. These two positions have different patterns of stacking interactions with aromatic residues present in the tunnel. Multiple patterns are not observed in nonprocessive endo-cellulases, where only one sugar position is favored by aromatic stacking. It is therefore proposed that the aromatic residues serve as lubricating agents to reduce the sliding barrier in the processive action.

PubMed: 10985769
DOI: 10.1021/bi001139p

Experimental method

X-RAY DIFFRACTION (2.3 Å)