1g66: Difference between revisions

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[[Image:1g66.jpg|left|200px]]
{{Seed}}
[[Image:1g66.png|left|200px]]


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{{STRUCTURE_1g66|  PDB=1g66  |  SCENE=  }}  
{{STRUCTURE_1g66|  PDB=1g66  |  SCENE=  }}  


'''ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION'''
===ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION===




==Overview==
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Acetylxylan esterase (AXEII; 207 amino acids) from Penicillium purpurogenum has substrate specificities toward acetate esters of d-xylopyranose residues in xylan and belongs to a new class of alpha/beta hydrolases. The crystal structure of AXEII has been determined by single isomorphous replacement and anomalous scattering, and refined at 0.90- and 1.10-A resolutions with data collected at 85 K and 295 K, respectively. The tertiary structure consists of a doubly wound alpha/beta sandwich, having a central six-stranded parallel beta-sheet flanked by two parallel alpha-helices on each side. The catalytic residues Ser(90), His(187), and Asp(175) are located at the C-terminal end of the sheet, an exposed region of the molecule. The serine and histidine side chains in the 295 K structure show the frequently observed conformations in which Ser(90) is trans and the hydroxyl group is in the plane of the imidazole ring of His(187). However, the structure at 85 K displays an additional conformation in which Ser(90) side-chain hydroxyl is away from the plane of the imidazole ring of His(187). The His(187) side chain forms a hydrogen bond with a sulfate ion and adopts an altered conformation. The only other known hydrolase that has a similar tertiary structure is Fusarium solani cutinase. The exposed nature of the catalytic triad suggests that AXEII is a pure esterase, i.e. an alpha/beta hydrolase with specificity for nonlipidic polar substrates.
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{{ABSTRACT_PUBMED_11134051}}


==About this Structure==
==About this Structure==
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[[Category: Ultra-high resolution]]
[[Category: Ultra-high resolution]]
[[Category: Xylan]]
[[Category: Xylan]]
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