Difference between revisions of "Part:BBa K5246031"
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===Usage and Biology=== | ===Usage and Biology=== | ||
TBA | TBA | ||
+ | |||
+ | <html> | ||
+ | <body> | ||
+ | <p> | ||
+ | This part also has a non his-tagged variant <a href="https://parts.igem.org/Part:BBa_K5246020">BBa_K5246020</a>. | ||
+ | </p> | ||
+ | </html> | ||
===Sequence and Features=== | ===Sequence and Features=== | ||
<partinfo>BBa_K5246031 SequenceAndFeatures</partinfo> | <partinfo>BBa_K5246031 SequenceAndFeatures</partinfo> | ||
− | |||
− | |||
− | |||
===Experimental characterization=== | ===Experimental characterization=== | ||
+ | ====Bioinformatic analysis==== | ||
+ | |||
+ | Conserved domain database analysis suggests that HfsH is part of the carbohydrate esterase 4 superfamily and polysaccharide deacetylase family. Proteins of this family may catalyze the N- or O- deacetylation of a substrate. Protein BLAST results show high similarity to peptidoglycan N-acetylglucosamine deacetylase and other polysaccharide deacetylases. | ||
+ | |||
+ | Topology analysis with DeepTMHMM and AlphaFold3 structure showed that HfsH is most probably a globular protein located in the cytoplasm. A pTM score above 0.5 suggests that the predicted overall structure may closely resemble the true protein fold, while ipTM indicates the accuracy of the subunit positioning within the complex. Values higher than 0.8 represent confident, high-quality predictions. | ||
+ | |||
+ | HfsH is a globular polysaccharide deacetylase that catalyses the deacetylation of N-acetylglucosamine in the holdfast synthesis pathway, previous research supports our conclusions. [1][2][3] | ||
===References=== | ===References=== | ||
+ | 1. Wan, Z. et al. (2013a) ‘The adhesive and cohesive properties of a bacterial polysaccharide adhesin are modulated by a deacetylase’, Molecular Microbiology, 88(3), pp. 486–500. doi:10.1111/mmi.12199. | ||
+ | <br> | ||
+ | 2. Toh, E., Kurtz, Harry D. and Brun, Y.V. (2008) ‘Characterization of the Caulobacter crescentus holdfast polysaccharide biosynthesis pathway reveals significant redundancy in the initiating glycosyltransferase and polymerase steps’, Journal of Bacteriology, 190(21), pp. 7219–7231. doi:10.1128/jb.01003-08. | ||
+ | <br> | ||
+ | 3. Liu, Q. et al. (2022) ‘The screening and expression of polysaccharide deacetylase from caulobacter crescentus and its function analysis’, Biotechnology and Applied Biochemistry, 70(2), pp. 688–696. doi:10.1002/bab.2390. |
Revision as of 14:38, 28 September 2024
HB HfsH Deacetylase, 6xHis tag for purification
Introduction
Usage and Biology
TBA
This part also has a non his-tagged variant BBa_K5246020.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 385
- 1000COMPATIBLE WITH RFC[1000]
Experimental characterization
Bioinformatic analysis
Conserved domain database analysis suggests that HfsH is part of the carbohydrate esterase 4 superfamily and polysaccharide deacetylase family. Proteins of this family may catalyze the N- or O- deacetylation of a substrate. Protein BLAST results show high similarity to peptidoglycan N-acetylglucosamine deacetylase and other polysaccharide deacetylases.
Topology analysis with DeepTMHMM and AlphaFold3 structure showed that HfsH is most probably a globular protein located in the cytoplasm. A pTM score above 0.5 suggests that the predicted overall structure may closely resemble the true protein fold, while ipTM indicates the accuracy of the subunit positioning within the complex. Values higher than 0.8 represent confident, high-quality predictions.
HfsH is a globular polysaccharide deacetylase that catalyses the deacetylation of N-acetylglucosamine in the holdfast synthesis pathway, previous research supports our conclusions. [1][2][3]
References
1. Wan, Z. et al. (2013a) ‘The adhesive and cohesive properties of a bacterial polysaccharide adhesin are modulated by a deacetylase’, Molecular Microbiology, 88(3), pp. 486–500. doi:10.1111/mmi.12199.
2. Toh, E., Kurtz, Harry D. and Brun, Y.V. (2008) ‘Characterization of the Caulobacter crescentus holdfast polysaccharide biosynthesis pathway reveals significant redundancy in the initiating glycosyltransferase and polymerase steps’, Journal of Bacteriology, 190(21), pp. 7219–7231. doi:10.1128/jb.01003-08.
3. Liu, Q. et al. (2022) ‘The screening and expression of polysaccharide deacetylase from caulobacter crescentus and its function analysis’, Biotechnology and Applied Biochemistry, 70(2), pp. 688–696. doi:10.1002/bab.2390.