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![[Figure 3]](dz5353fig3mag.jpg)
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Figure 3
(a) The single-domain (α/α)6 fold of BT2949 viewed along the barrel axis. The barrel appears relatively undecorated, with only four major loops (shown in grey) comprising two small elements of secondary structure (shown in blue). (b) Surface view of BT2949 [identical orientation to that in (a)] coloured by sequence conservation using the alignment shown in Fig. 4 ![[link]](../../../../../../logos/arrows/d_arr.gif) (a); colour intensity indicates strongest conservation. The position of the proposed catalytic active site in (a) and (b) is indicated via an arrow and the view shown in (c) via a boxed region. (c) Divergent stereo image showing HEPES bound in BT3782 (PDB entry 4mu9, coloured grey) and α-1,6-mannobiose in BcGH76 (PDB entry 4boj, coloured coral) overlaid with BT2949 (green). HEPES makes a hydrogen-bonding interaction with Asp143 (all labels correspond to BT2949 numbering) and appears in close proximity to other likely substrate-coordinating residues. Mannobiose appears to occupy two distal subsites away from the proposed catalytic pair. Conserved residues from all enzyme models are shown overlaid. (a) was assembled using PyMOL v.1.6 (Schrödinger). Conservation mapping in (b) was conducted using Homolmapper (Rockwell & Lagarias, 2007) using the native structure of BT2949 and the sequence alignment in Fig. 4(a) as inputs. (b) and (c) were assembled using CCP4mg (McNicholas et al., 2011). |
![[Figure 3]](dz5353fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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