 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](tb5084fig2mag.jpg)
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Figure 2
Structure alignment of the CA_C0359 protein with YteR (PDB entry 2gh4) and comparison of conserved active residues in the catalytic site. (a) CA_C0359 (cyan) aligned with the structure of YteR (red) with an r.m.s.d. of 1.4 Å; the protruding loop of CA_C0359 is boxed in black. (b) A comparison of active residue location of YteR with conserved residues of CA_C0359 on the protein alignment of CA_C0359 and YteR (gray), with the protruding loop of CA_C0359 colored magenta. Unsaturated rhamnogalacturonan, indicated by the red and cyan sticks, is bound to YteR (PDB entry 2gh4). The YteR residues highlighted in blue are Asp143, His189, Asp88, Tyr41 and Lys133. The conserved CA_C0359 residues labelled in red and highlighted in green include Asp130, His176, Asp75, Tyr25 and Lys120 and are seen to align well with the analogous YteR residues. Two additional lysines, Lys325 and Lys346, of CA_C0359 have been computationally determined to interact and coordinate substrate binding. |
![[Figure 2]](tb5084fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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