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Novel clostridial c...
Novel clostridial cell-surface hemicellulose-binding CBM3 proteins
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Hershko Rimon, Almog (författare)
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Livnah, Oded (författare)
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- Rozman Grinberg, Inna (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Tel Aviv University, Israel
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Ortiz de Ora, Lizett (författare)
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Yaniv, Oren (författare)
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Lamed, Raphael (författare)
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Bayer, Edward A. (författare)
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Frolow, Felix (författare)
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Voronov-Goldman, Milana (författare)
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(creator_code:org_t)
- 2021
- 2021
- Engelska.
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Ingår i: Acta Crystallographica Section F. - 2053-230X. ; 77, s. 95-104
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- A novel member of the family 3 carbohydrate-binding modules (CBM3s) is encoded by a gene (Cthe_0271) in Clostridium thermocellum which is the most highly expressed gene in the bacterium during its growth on several types of biomass substrates. Surprisingly, CtCBM3-0271 binds to at least two different types of xylan, instead of the common binding of CBM3s to cellulosic substrates. CtCBM3-0271 was crystallized and its three-dimensional structure was solved and refined to a resolution of 1.8 angstrom. In order to learn more about the role of this type of CBM3, a comparative study with its orthologue from Clostridium clariflavum (encoded by the Clocl_1192 gene) was performed, and the three-dimensional structure of CcCBM3-1192 was determined to 1.6 angstrom resolution. Carbohydrate binding by CcCBM3-1192 was found to be similar to that by CtCBM3-0271; both exhibited binding to xylan rather than to cellulose. Comparative structural analysis of the two CBM3s provided a clear functional correlation of structure and binding, in which the two CBM3s lack the required number of binding residues in their cellulose-binding strips and thus lack cellulose-binding capabilities. This is an enigma, as CtCBM3-0271 was reported to be a highly expressed protein when the bacterium was grown on cellulose. An additional unexpected finding was that CcCBM3-1192 does not contain the calcium ion that was considered to play a structural stabilizing role in the CBM3 family. Despite the lack of calcium, the five residues that form the calcium-binding site are conserved. The absence of calcium results in conformational changes in two loops of the CcCBM3-1192 structure. In this context, superposition of the non-calcium-binding CcCBM3-1192 with CtCBM3-0271 and other calcium-binding CBM3s reveals a much broader two-loop region in the former compared with CtCBM3-0271.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- cellulosome
- CBM
- calcium binding
- crystal structure
- Clostridium thermocellum
- Clostridium clariflavum
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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