2HL6

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

Summary for 2HL6

• Entry DOI: 10.2210/pdb2hl6/pdb
• Descriptor: Feruloyl esterase A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: esterase, a/b hydrolase fold, glycosylated, caps, hydrolase
• Biological source: Aspergillus niger
• Cellular location: Secreted: O42807
• Total number of polymer chains: 2
• Total formula weight: 59566.63

Authors

Parsiegla, G.,Herpoel-Gimbert, I.,Dubots, J. (deposition date: 2006-07-06, release date: 2006-10-31, Last modification date: 2024-11-06)

Primary citation

Benoit, I.,Asther, M.,Sulzenbacher, G.,Record, E.,Marmuse, L.,Parsiegla, G.,Herpoel-Gimbert, I.,Asther, M.,Bignon, C.
Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A
Febs Lett., 580:5815-5821, 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 (1.55 Å)