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File:GH3 2013 Fig4.png
Revision as of 11:36, 10 April 2013 by Brian Mark (talk | contribs) ('''Figure 4.''' '''Overlay of barley β-glucan exohydrolase isoenzyme ExoI (domain 1 in magenta, and domain 2 in cyan) with the two-domain GH3 NagZ from ''B. subtilis'' (BsNagZ) (yellow) (PDB: 3BMX). '''GH3 NagZ enzymes contain a conse...)
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GH3_2013_Fig4.png (720 × 540 pixels, file size: 356 KB, MIME type: image/png)
Figure 4. Overlay of barley β-glucan exohydrolase isoenzyme ExoI (domain 1 in magenta, and domain 2 in cyan) with the two-domain GH3 NagZ from B. subtilis (BsNagZ) (yellow) (PDB: 3BMX). GH3 NagZ enzymes contain a conserved histidine/aspartate dyad within a flexible loop of the catalytic domain that has been proposed as the general acid/base. In contrast to Exo1, the additional domain of BsNagZ does not participate in catalysis. The catalytic Asp nucleophile however, is conserved across the GH3 family, including the NagZ enzymes.
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 11:36, 10 April 2013 | | 720 × 540 (356 KB) | Brian Mark (talk | contribs) | '''Figure 4.''' '''Overlay of barley β-glucan exohydrolase isoenzyme ExoI (domain 1 in magenta, and domain 2 in cyan) with the two-domain GH3 NagZ from ''B. subtilis'' (BsNagZ) (yellow) (PDB: 3BMX). '''GH3 NagZ enzymes contain a conse... |
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