5CVY
The Structure of Bacillus pumilus GH48 in complex with cellobiose and cellohexaose
Summary for 5CVY
| Entry DOI | 10.2210/pdb5cvy/pdb |
| Related PRD ID | PRD_900005 PRD_900020 |
| Descriptor | Glycoside hydrolase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | cellulase, hydrolase |
| Biological source | Bacillus pumilus (strain SAFR-032) |
| Total number of polymer chains | 1 |
| Total formula weight | 83196.17 |
| Authors | Alahuhta, P.M.,Lunin, V.V. (deposition date: 2015-07-27, release date: 2016-08-10, Last modification date: 2023-09-27) |
| Primary citation | Brunecky, R.,Alahuhta, M.,Sammond, D.W.,Xu, Q.,Chen, M.,Wilson, D.B.,Brady, J.W.,Himmel, M.E.,Bomble, Y.J.,Lunin, V.V. Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure. Biotechnol Biofuels, 10:274-274, 2017 Cited by PubMed Abstract: Glycoside hydrolase (GH) family 48 is an understudied and increasingly important exoglucanase family found in the majority of bacterial cellulase systems. Moreover, many thermophilic enzyme systems contain GH48 enzymes. Deletion of GH48 enzymes in these microorganisms results in drastic reduction in biomass deconstruction. Surprisingly, given their importance for these microorganisms, GH48s have intrinsically low cellulolytic activity but even in low ratios synergize greatly with GH9 endoglucanases. In this study, we explore the structural and enzymatic diversity of these enzymes across a wide range of temperature optima. We have crystallized one new GH48 module from in a complex with cellobiose and cellohexaose (GH48). We compare this structure to other known GH48 enzymes in an attempt to understand GH48 structure/function relationships and draw general rules correlating amino acid sequences and secondary structures to thermostability in this GH family. PubMed: 29213319DOI: 10.1186/s13068-017-0951-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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