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Structure of CBM4 from Clostridium thermocellum cellulase K.

ABSTRACT: Here, a 2.0 Å 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.

SUBMITTER: Alahuhta M

PROVIDER: S-EPMC3087633 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Structure of CBM4 from Clostridium thermocellum cellulase K.

Alahuhta Markus M Luo Yonghua Y Ding Shi You SY Himmel Michael E ME Lunin Vladimir V VV

Acta crystallographica. Section F, Structural biology and crystallization communications 20110420 Pt 5

Here, a 2.0 Å 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 th ...[more]

PMID: 21543854

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2018-09-05 | PXD009882 | Pride

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