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| - | [[Image:1qk0.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1qk0| PDB=1qk0 | SCENE= }} | | {{STRUCTURE_1qk0| PDB=1qk0 | SCENE= }} |
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| - | '''CEL6A IN COMPLEX WITH M-IODOBENZYL BETA-D-GLUCOPYRANOSYL-BETA(1,4)-D-XYLOPYRANOSIDE'''
| + | ===CEL6A IN COMPLEX WITH M-IODOBENZYL BETA-D-GLUCOPYRANOSYL-BETA(1,4)-D-XYLOPYRANOSIDE=== |
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| - | ==Overview==
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| - | BACKGROUND: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The catalytic core has a structure that is a variation of the classic TIM barrel. The active site is located inside a tunnel, the roof of which is formed mainly by a pair of loops. RESULTS: We describe three new ligand complexes. One is the structure of the wild-type enzyme in complex with a nonhydrolysable cello-oligosaccharide, methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside (Glc)(2)-S-(Glc)(2), which differs from a cellotetraose in the nature of the central glycosidic linkage where a sulphur atom replaces an oxygen atom. The second structure is a mutant, Y169F, in complex with the same ligand, and the third is the wild-type enzyme in complex with m-iodobenzyl beta-D-glucopyranosyl-beta(1,4)-D-xylopyranoside (IBXG). CONCLUSIONS: The (Glc)(2)-S-(Glc)(2) ligand binds in the -2 to +2 sites in both the wild-type and mutant enzymes. The glucosyl unit in the -1 site is distorted from the usual chair conformation in both structures. The IBXG ligand binds in the -2 to +1 sites, with the xylosyl unit in the -1 site where it adopts the energetically favourable chair conformation. The -1 site glucosyl of the (Glc)(2)-S-(Glc)(2) ligand is unable to take on this conformation because of steric clashes with the protein. The crystallographic results show that one of the tunnel-forming loops in Cel6A is sensitive to modifications at the active site, and is able to take on a number of different conformations. One of the conformational changes disrupts a set of interactions at the active site that we propose is an integral part of the reaction mechanism.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10508787}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10508787 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10508787}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glycoprotein]] | | [[Category: Glycoprotein]] |
| | [[Category: Glycosidase]] | | [[Category: Glycosidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:21:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:39:35 2008'' |
Revision as of 02:39, 29 July 2008
Template:STRUCTURE 1qk0
CEL6A IN COMPLEX WITH M-IODOBENZYL BETA-D-GLUCOPYRANOSYL-BETA(1,4)-D-XYLOPYRANOSIDE
Template:ABSTRACT PUBMED 10508787
About this Structure
1QK0 is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.
Reference
Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei., Zou J, Kleywegt GJ, Stahlberg J, Driguez H, Nerinckx W, Claeyssens M, Koivula A, Teeri TT, Jones TA, Structure. 1999 Sep 15;7(9):1035-45. PMID:10508787
Page seeded by OCA on Tue Jul 29 05:39:35 2008
