1e5n
From Proteopedia
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'''E246C MUTANT OF P FLUORESCENS SUBSP. CELLULOSA XYLANASE A IN COMPLEX WITH XYLOPENTAOSE''' | '''E246C MUTANT OF P FLUORESCENS SUBSP. CELLULOSA XYLANASE A IN COMPLEX WITH XYLOPENTAOSE''' | ||
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[[Category: Leggio, L Lo.]] | [[Category: Leggio, L Lo.]] | ||
[[Category: Pickersgill, R W.]] | [[Category: Pickersgill, R W.]] | ||
| - | [[Category: | + | [[Category: Family 10]] |
| - | [[Category: | + | [[Category: Glycosyl hydrolase]] |
| - | [[Category: | + | [[Category: Tim barrel]] |
| - | [[Category: | + | [[Category: Xylan degradation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:41:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:41, 2 May 2008
E246C MUTANT OF P FLUORESCENS SUBSP. CELLULOSA XYLANASE A IN COMPLEX WITH XYLOPENTAOSE
Overview
The structure of the complex between a catalytically compromised family 10 xylanase and a xylopentaose substrate has been determined by X-ray crystallography and refined to 3.2 A resolution. The substrate binds at the C-terminal end of the eightfold betaalpha-barrel of Pseudomonas fluorescens subsp. cellulosa xylanase A and occupies substrate binding subsites -1 to +4. Crystal contacts are shown to prevent the expected mode of binding from subsite -2 to +3, because of steric hindrance to subsite -2. The loss of accessible surface at individual subsites on binding of xylopentaose parallels well previously reported experimental measurements of individual subsites binding energies, decreasing going from subsite +2 to +4. Nine conserved residues contribute to subsite -1, including three tryptophan residues forming an aromatic cage around the xylosyl residue at this subsite. One of these, Trp 313, is the single residue contributing most lost accessible surface to subsite -1, and goes from a highly mobile to a well-defined conformation on binding of the substrate. A comparison of xylanase A with C. fimi CEX around the +1 subsite suggests that a flatter and less polar surface is responsible for the better catalytic properties of CEX on aryl substrates. The view of catalysis that emerges from combining this with previously published work is the following: (1) xylan is recognized and bound by the xylanase as a left-handed threefold helix; (2) the xylosyl residue at subsite -1 is distorted and pulled down toward the catalytic residues, and the glycosidic bond is strained and broken to form the enzyme-substrate covalent intermediate; (3) the intermediate is attacked by an activated water molecule, following the classic retaining glycosyl hydrolase mechanism.
About this Structure
1E5N is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
X-ray crystallographic study of xylopentaose binding to Pseudomonas fluorescens xylanase A., Leggio LL, Jenkins J, Harris GW, Pickersgill RW, Proteins. 2000 Nov 15;41(3):362-73. PMID:11025547 Page seeded by OCA on Fri May 2 14:41:43 2008
