2hl6

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(New page: 200px<br /><applet load="2hl6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hl6, resolution 1.550&Aring;" /> '''Structure of homolo...)
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Revision as of 09:42, 21 November 2007

Image:2hl6.gif

2hl6, resolution 1.550Å

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Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex with CAPS

Overview

The thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied., From the most to the least thermo-resistant, the four molecular species, ranked as follows: (i) glycosylated form produced native, (ii), non-glycosylated form produced native, (iii) non-glycosylated form, produced as inclusion bodies and refolded, and (iv) glycosylated form, produced native chemically denatured and then refolded. On the basis of, these results and of crystal structure data, we discuss the respective, importance of protein folding and glycosylation in the thermal stability, of recombinant FAEA.

About this Structure

2HL6 is a Single protein structure of sequence from Aspergillus niger with SO4, EDO and CXS as ligands. Active as Feruloyl esterase, with EC number 3.1.1.73 Full crystallographic information is available from OCA.

Reference

Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A., Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C, FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:17027758

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