Structure of CBM4 from Clostridium thermocellum cellulase K

被引:8
作者
Alahuhta, Markus [1 ]
Luo, Yonghua [1 ]
Ding, Shi-You [1 ]
Himmel, Michael E. [1 ]
Lunin, Vladimir V. [1 ]
机构
[1] Natl Renewable Energy Lab, BioSci Ctr, Golden, CO 80401 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷
关键词
CARBOHYDRATE-BINDING MODULES;
D O I
10.1107/S1744309111003307
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Here, a 2.0 angstrom resolution X-ray structure of Clostridium thermocellum cellulase K family 4 carbohydrate-binding module (CelK CBM4) is reported. The resulting structure was refined to an R factor of 0.212 and an R-free of 0.274. Structural analysis shows that this new structure is very similar to the previously solved structure of C. thermocellum CbhA CBM4. Most importantly, these data support the previously proposed notion of an extended binding pocket using a novel tryptophan-containing loop that may be highly conserved in clostridial CBM4 proteins.
引用
收藏
页码:527 / 530
页数:4
相关论文
共 13 条
[11]   Refinement of macromolecular structures by the maximum-likelihood method [J].
Murshudov, GN ;
Vagin, AA ;
Dodson, EJ .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1997, 53 :240-255
[12]   Molecular replacement with MOLREP [J].
Vagin, Alexei ;
Teplyakov, Alexei .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2010, 66 :22-25
[13]   The binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana:: differences in β-glucan binding within family CBM4 [J].
Zverlov, VV ;
Volkov, IY ;
Velikodvorskaya, GA ;
Schwarz, WH .
MICROBIOLOGY-SGM, 2001, 147 :621-629