2hl6 | pdb_00002hl6

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

spinqualitylabelsall models 2hl6, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hl6 is a 2 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, CXS, EDO, SO4, MAN, NAG Gene: faeA (Aspergillus niger) Activity: Feruloyl esterase, with EC number 3.1.1.73 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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