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Fig. 2 | Bioresources and Bioprocessing

Fig. 2

From: A novel accessory protein ArCel5 from cellulose-gelatinizing fungus Arthrobotrys sp. CX1

Fig. 2

Sequence and structure properties of ArCel5. a Alignment of amino acid sequences of ArCel5 (GenBank accession number MN654111), Ta_Cel5A (GenBank accession number AAL88714.2), AnCel5A (GenBank accession number AF331518.1) and RBCel1(GenBank accession number ACO55737). The signal peptide (dotted line), family 1 carbohydrate-binding molecule (gray full line) and linker peptide (black full line) of ArCel5 were also marked. The amino acid residues conserved in all four proteins are shown with white letters and black boxes, and the amino acid residues conserved in two or three differential protein are shown with highlighted in gray, and the secondary structure is shown above the sequence. Sequence alignment was analyzed by ClustalOmega (Petersen et al. 2011), and results were output by Espript 3 server (Patrice et al. 2003). b ArCel5 structure was shown in a cartoon model with the CBM, linker, and CD domain in blue, red and green, respectively. c A structural overlay of the modeled ArCel5 with AnCel5A (PDB entry 5i77, orange) was made to allow visual comparison. d Structure comparison of TrCBM1 (PDB entry 1CBH, orange) with ArCel5-CBM (blue). e ArCel5-CBM and TrCBM1 could form a flat binding surface with cellulose, and the three conserved tyrosines were shown in yellow and gray, respectively. The structure homology-modeling of ArCel5 was predicted by using I-TASSER online server (http://zhanglab.ccmb.med.umich.edu/I-TASSER/)

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