3W6L
Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase
Summary for 3W6L
| Entry DOI | 10.2210/pdb3w6l/pdb |
| Related | 2zun 3W6M 3axx 3qhm 3qhn 3qho |
| Descriptor | 458aa long hypothetical endo-1,4-beta-glucanase, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | hyperthermophilic, disulfide bond, tim barrel, glycosyl hydrolase, hydrolizaiton, membrane-bound, hydrolase |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 3 |
| Total formula weight | 131296.43 |
| Authors | Kim, H.-W.,Ishikawa, K. (deposition date: 2013-02-15, release date: 2013-05-29, Last modification date: 2024-10-30) |
| Primary citation | Kim, H.-W.,Ishikawa, K. The role of disulfide bond in hyperthermophilic endocellulase Extremophiles, 17:593-599, 2013 Cited by PubMed Abstract: The hyperthermophilic endocellulase, EGPh (glycosyl hydrolase family 5) from Pyrococcus horikoshii possesses 4 cysteine residues forming 2 disulfide bonds, as identified by structural analysis. One of the disulfide bonds is located at the proximal region of the active site in EGPh, which exhibits a distinct pattern from that of the thermophilic endocellulase EGAc (glycosyl hydrolase family 5) of Acidothermus cellulolyticus despite the structural similarity between the two endocellulases. The structural similarity between EGPh and EGAc suggests that EGPh possesses a structure suitable for changing the position of the disulfide bond corresponding to that in EGAc. Introduction of this alternative disulfide bond in EGPh, while removing the original disulfide bond, did not result in a loss of enzymatic activity but the EGPh was no longer hyperthermostable. These results suggest that the contribution of disulfide bond to hyperthermostability at temperature higher than 100 °C is restrictive, and that its impact is dependent on the specific structural environment of the hyperthermophilic proteins. The data suggest that the structural position and environment of the disulfide bond has a greater effect on high-temperature thermostability of the enzyme than on the potential energy of the dihedral angle that contributes to disulfide bond cleavage. PubMed: 23624891DOI: 10.1007/s00792-013-0542-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.751 Å) |
Structure validation
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