A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly.

No abstract is available for this paper.

• Publication year

  1997

• Venue

  Structure

• Publication date

  1997-03-15

• Fields of study

  Biology, Medicine, Materials Science, Chemistry

• Identifiers
  DOI 10.1016/S0969-2126(97)00195-0PMID 9083107
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The cellulose paradox: pollutant par excellence and/or a reclaimable natural resource?

  2004cited by this paper
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  1996cited by this paper
• Bacterial adhesion : molecular and ecological diversity

  1996cited by this paper
• Expression, purification and crystallization of a cohesin domain from the cellulosome of Clostridium thermocellum.

  1996cited by this paper
• Structural role of calcium for the organization of the cellulosome of Clostridium thermocellum.

  1996cited by this paper
• The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation.

  1996cited by this paper
• Interaction between the endoglucanase CelA and the scaffolding protein CipC of the Clostridium cellulolyticum cellulosome

  1996cited by this paper
• Crystal structure of a bacterial family‐III cellulose‐binding domain: a general mechanism for attachment to cellulose.

  1996cited by this paper
• Cellulose hydrolysis by bacteria and fungi.

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• Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy

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• Expression, purification and subunit‐binding properties of cohesins 2 and 3 of the Clostridium thermocellum cellulosome

  1995cited by this paper
• Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy.

  1995cited by this paper
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  1994cited by this paper
• Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome-integrating protein CipA

  1994cited by this paper
• The cellulose‐binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding

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• The Clostridium cellulovorans cellulosome.

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• The cellulosome--a treasure-trove for biotechnology.

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• The CCP4 suite: programs for protein crystallography.

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• Protein structure comparison by alignment of distance matrices.

  1993cited by this paper
• Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL‐protein reveals an unusual degree of internal homology

  1993influential reference
• The hydrophobic repeated domain of the Clostridium cellulovorans cellulose-binding protein (CbpA) has specific interactions with endoglucanases

  1993cited by this paper
• The nature of the carbohydrate-peptide linkage region in glycoproteins from the cellulosomes of Clostridium thermocellum and Bacteroides cellulosolvens.

  1993cited by this paper
• Properties conferred on Clostridium thermocellum endoglucanase CelC by grafting the duplicated segment of endoglucanase CelD.

  1993cited by this paper
• Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

  1992cited by this paper
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  1992cited by this paper
• Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS.

  1992cited by this paper
• Unorthodox intrasubunit interactions in the cellulosome ofClostridium thermocellum

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• Anomalous dissociative behavior of the major glycosylated component of the cellulosome of clostridium thermocellum

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  2018cites this paper
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