Structure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82Å resolution

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 69, Issue 12, 2013, Pages 1335-1338

  Alahuhta, Markus ^a   Adney, William S ^a   Himmel, Michael E ^a   Lunin, Vladimir V ^a  

^a NATIONAL RENEWABLE ENERGY LABORATORY   (United States)

Author keywords

endoglucanases; GH74; glycoside hydrolases; xyloglucanases

Indexed keywords

BACTERIAL PROTEIN; GLYCOSIDASE; RECOMBINANT PROTEIN; XYLOGLUCAN ENDO(1 4) BETA D GLUCANASE; XYLOGLUCAN ENDO(1-4)-BETA-D-GLUCANASE;

ACTINOMYCETALES; AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CLOSTRIDIUM THERMOCELLUM; ENDOGLUCANASES; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; GEOTRICHUM; GH74; METABOLISM; MOLECULAR GENETICS; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY; XYLOGLUCANASES;

ENDOGLUCANASES; GH74; GLYCOSIDE HYDROLASES; XYLOGLUCANASES;

ACTINOMYCETALES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CLOSTRIDIUM THERMOCELLUM; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GENE EXPRESSION; GEOTRICHUM; GLYCOSIDE HYDROLASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 84890050923     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309113030005     Document Type: Article

References (21)

1. Cantarel, B. L., Coutinho, P. M., Rancurel, C., Bernard, T., Lombard, V. & Henrissat, B. (2009). Nucleic Acids Res. 37, D233-D238.
2. Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Cryst. D66, 12-21.
3. Ding, S.-Y., Adney, W. S., Vinzant, T. B., Decker, S. R., Baker, J. O., Thomas, S. R. & Himmel, M. E. (2003). ACS Symp. Ser. 855, 332-360.
4. Ding, S.-Y., Adney, W. S., Vinzant, T. B. & Himmel, M. E. (2008). US Patent 7364890.
5. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
6. Engh, R. A. & Huber, R. (1991). Acta Cryst. A47, 392-400.
7. Fry, S. C. (1989). J. Exp. Bot. 40, 1-11.
8. Hayashi, T. (1989). Annu. Rev. Plant Physiol. 40, 139-168.
9. Hayashi, T. & Kaida, R. (2011). Mol. Plant, 4, 17-24.
10. Krissinel, E. & Henrick, K. (2004). Acta Cryst. D60, 2256-2268.
11. Lovell, S. C., Davis, I.W., Arendall, W. B., de Bakker, P. I., Word, J. M., Prisant, M. G., Richardson, J. S. & Richardson, D. C. (2003). Proteins, 50, 437-450.
12. Martinez-Fleites, C., Guerreiro, C. I. P. D., Baumann, M. J., Taylor, E. J., Prates, J. A. M., Ferreira, L. M. A., Fontes, C. M. G. A., Brumer, H. & Davies, G. J. (2006). J. Biol. Chem. 281, 24922-24933.
13. McCarter, J. D. & Withers, S. G. (1994). Curr. Opin. Struct. Biol. 4, 885-892.
14. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
15. Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Sö ding, J., Thompson, J. D. & Higgins, D. G. (2011). Mol. Syst. Biol. 7, 539.
16. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
17. Vincken, J.-P., York, W. S., Beldman, G. & Voragen, A. G. J. (1997). Plant Physiol. 114, 9-13.
18. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
19. Yaoi, K., Kondo, H., Hiyoshi, A., Noro, N., Sugimoto, H., Tsuda, S., Mitsuishi, Y. & Miyazaki, K. (2007). J. Mol. Biol. 370, 53-62.
20. Yaoi, K., Kondo, H., Hiyoshi, A., Noro, N., Sugimoto, H., Tsuda, S. & Miyazaki, K. (2009). FEBS J. 276, 5094-5100.
21. Yaoi, K., Kondo, H., Noro, N., Suzuki, M., Tsuda, S. & Mitsuishi, Y. (2004). Structure, 12, 1209-1217.