. 2018 Apr 26;13(4):e0196358. doi: 10.1371/journal.pone.0196358

Table 3. Comparison of GH43 family β-1,4-xylosidases.

β-1,4-Xylosidase^†	Oligomeric state in asymmetric unit	RMSD (Å) ^‡	Sequence identity to Xyl (%)^§
β-1,4-Xylosidase^†	Oligomeric state in asymmetric unit	RMSD (Å) ^‡	Full length	N-terminal domain	C-terminal domain
Gthe	1	0.290	100.0	100.0	100.0
Gste	4	1.262	35.2	40.5	27.3
Cace	4	1.345	35.0	39.8	28.8
Bhal	2	1.267	34.8	40.7	25.9
Srum	4	1.279	34.6	38.5	28.7
Bsub	4	1.305	33.9	41.8	22.9

^† The β-1,4-xylosidases are from G. thermoleovorans IT-08 (Gthe; GenPept ABC75004; Xyl), G. stearothermophilus T-6 (Gste; GenPept AA98625; PDB 2EXH), C. acetobutylicum ATCC 824 (Cace; GenPept AAK81382; PDB 1YI7), B. halodurans C-125 (Bhal; GenPept BAB07402; PDB 1YRZ), S. ruminantium GA192 (Srum; GenPept AAB97967; PDB 3C2U), and B. subtilis subsp. subtilis str. 168 (Bsub; GenPept AAB41091; PDB 1YIF).

^‡ Root-mean-square deviations between Cα atoms of pairwise structural alignments of the β-1,4-xylosidases with the Xyl structure as template. The RMSD for Gthe β-1,4-xylosidase is the average RMSD between the Xyl•arabinose, Xyl•xylose, and Xyl•arabinose•xylose structures; for the other enzymes, the RMSD is the average RMSD of the superposition with all available sub-unit structures. The structural alignments were performed using the Secondary Structure Matching (SSM) server [31].

^§ The N-terminal domain contains the amino acid residues equivalent to residues 1–304 of Xyl, while the C-terminal domain contains the residues that correspond to residues 310–511 of Xyl.