2IX9

Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A

Summary for 2IX9

• Entry DOI: 10.2210/pdb2ix9/pdb
• Related: 1USW 1UWC 1UZA 2BJH
• Descriptor: FERULOYL ESTERASE A, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: hydrolase, xylan degradation, feruloyl esterase ec 3.1.1.73, glycoprotein, serine esterase
• Biological source: ASPERGILLUS NIGER
• Cellular location: Secreted: O42807
• Total number of polymer chains: 2
• Total formula weight: 57877.14

Authors

Sulzenbacher, G.,Benoit, I. (deposition date: 2006-07-07, release date: 2006-10-18, Last modification date: 2024-10-23)

Primary citation

Benoit, I.,Asther, M.,Sulzenbacher, G.,Record, E.,Marmuse, L.,Parsiegla, G.,Gimbert, I.,Asther, M.,Bignon, C.
Respective Importance of Protein Folding and Glycosylation in the Thermal Stability of Recombinant Feruloyl Esterase A.
FEBS Lett., 580:5815-, 2006

PubMed Abstract: 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.

PubMed: 17027758
DOI: 10.1016/J.FEBSLET.2006.09.039

Experimental method

X-RAY DIFFRACTION (1.7 Å)