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4Q7Q’s inclusion in this family also supports its SPRITE-derived hypothetical functionality. Rhamnogalacturonan Acetylesterase—the enzyme with one of the best SPRITE-based alignment relative to 4Q7Q—is a member of this family.F Proteins in this family are also known for containing a “unique hydrogen bond network that [stabilizes]” the active site.F
4Q7Q’s inclusion in this family also supports its SPRITE-derived hypothetical functionality. Rhamnogalacturonan Acetylesterase—the enzyme with one of the best SPRITE-based alignment relative to 4Q7Q—is a member of this family.F Proteins in this family are also known for containing a “unique hydrogen bond network that [stabilizes]” the active site.F
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Regarding what protein family 4Q7Q belongs to, DALI results suggest it is a part of a sub-family of the greater GDSL/SGNH superfamily. A PDB90% DALI search labels 4Q7Q as a part of the “Lipolytic Protein G-D-S-L Family,” which refers to enzymes that hydrolyze lipid substrates.I
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Regarding what protein family 4Q7Q belongs to, DALI results suggest it is a part of a sub-family of the greater GDSL/SGNH superfamily. A PDB90% DALI search labels 4Q7Q as a part of the “Lipolytic Protein G-D-S-L Family,” which refers to enzymes that hydrolyze lipid substrates.
== Sequence Analysis (DONE) ==
== Sequence Analysis (DONE) ==
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== Theoretical Functionality and Proposed Bodily Purpose ==
== Theoretical Functionality and Proposed Bodily Purpose ==
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''Highlight the data that helped you come to your conclusion here including any relevant figures. Make sure include potential substrates and binding sites.''
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According to our research the likely function of this protein is to break down bonds in mannans, glucomannans and galactomannans. The potential substrates and binding sites: 4-Nitrophenyl N-acetyl-β-D-glucosaminide, 4-Nitrophenyl α-D-glucopyranoside, and P-Nitrophenyl Phosphate
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Potential Substrates and Binding Sites: 4-Nitrophenyl N-acetyl-β-D-glucosaminide, 4-Nitrophenyl α-D-glucopyranoside, and P-Nitrophenyl Phosphate
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</StructureSection>
</StructureSection>
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== References ==
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== References (DONE) ==
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A) 1WAB. Protein Database, 1997. https://www.rcsb.org/structure/1WAB
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A) Dhawan, S.; Kaur, J.; Microbial Mannanases: An Overview of Production and Applications. Critical Reviews in Biotechnology 2007, 27, 197-216. DOI: 10.1080/07388550701775919
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B) Ho, Y. S.; Sewnson, L.; Derewenda, U.; Serre, L.; Wei, Y.; Dauter, Z.; Hattori, M.; Adachi, T.; Aoki, J.; Arai, H.; Inoue, K.; Derewenda, Z. S. Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer. Nature, 1997, 385, 89-93. https://www.nature.com/articles/385089a0 https://www.nature.com/articles/385089a0
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B) Soni, H.; Rawat, H. K.; Pletschke, B. I.; Kango, N. Purification and characterization of Beta-mannanase from Aspergillus terreus and its applicability in depolymerization of mannans and saccharification of lignocellulosic biomass. Biotech 2016, 6, 136. DOI: 10.1007/s13205-016-0454-2
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C) Miesfeld, R. L.; McEvoy, M. M. Biochemistry, 2nd ed.; W. W. Norton & Company, 2021.
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C) Cheng, L.; Duan, S.; Feng, X.; Zheng, K.; Yang, Q.; Liu, Z. Purification and Characterization of a Thermostable Beta-Mannanase from Bacillus subtilis BE-91: Potential Application in Inflammatory Diseases. BioMed Research International 2016, 2016, 1-7. DOI: 10.1155/2016/6380147
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D) SGNH hydrolase superfamily. InterPro, 2017. https://www.ebi.ac.uk/interpro/entry/InterPro/IPR036514/
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E) Molgaard, A.; Kauppinen, S.; Larsen, S. Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Struct., 2000, 8(4), 373-383. https://www.sciencedirect.com/science/article/pii/S0969212600001180?via%3Dihub
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F) 4Q7Q. Protein Database, 2014. https://www.rcsb.org/structure/4Q7Q
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G) Rio, T. G. D.; et al. Complete genome sequence of Chitinophaga pinensis type strain (UQM 2034). Stand. Genomic. Sci., 2010, 2(1), 87-95. https://pmc.ncbi.nlm.nih.gov/articles/PMC3035255/
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H) Akoh, C. C.; Lee, G.; Liaw, Y.; Huang, T.; Shaw, J. GDSL family of serine esterases/lipases. Prog. Lipid Res., 2004, 43(6), 534-552. https://pubmed.ncbi.nlm.nih.gov/15522763/
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I) 7BXD. Protein Database, 2021. https://www.rcsb.org/structure/7BXD
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J) Madej,T.; Lanczycki, C. J.; Zhang, D.; Thiessen, P. A.; Geer, R. C.; Marchler-Bauer, A.; Bryant, S. H. MMDB and VAST+: tracking structural similarities between macromolecular complexes. Nucleic Acids Res., 2014, 42(Database), D297-303. https://doi.org/10.1093/nar/gkt1208
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<references/>
<references/>

Revision as of 02:46, 28 April 2025

3CBW Structure and Proposed Functionality

(NOTE TO ALL EDITORS: This page is part of a final project for a biochemistry lab at Elizabethtown College. Please do not edit this.)

3CBW is a homodimeric protein complex that originates from the bacterial species Chitinophaga Pinensis and has a mass of 80.65 kDa. It is a member of the SGNH Hydrolase Superfamily with structural and sequential similarities to esterases and lipases. Current evidence suggests it causes the hydrolysis of esters and/or acetyl groups on lipids/lipid-like molecules via a serine protease-like active site.

PDB ID 3CBW

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References (DONE)

A) Dhawan, S.; Kaur, J.; Microbial Mannanases: An Overview of Production and Applications. Critical Reviews in Biotechnology 2007, 27, 197-216. DOI: 10.1080/07388550701775919 B) Soni, H.; Rawat, H. K.; Pletschke, B. I.; Kango, N. Purification and characterization of Beta-mannanase from Aspergillus terreus and its applicability in depolymerization of mannans and saccharification of lignocellulosic biomass. Biotech 2016, 6, 136. DOI: 10.1007/s13205-016-0454-2 C) Cheng, L.; Duan, S.; Feng, X.; Zheng, K.; Yang, Q.; Liu, Z. Purification and Characterization of a Thermostable Beta-Mannanase from Bacillus subtilis BE-91: Potential Application in Inflammatory Diseases. BioMed Research International 2016, 2016, 1-7. DOI: 10.1155/2016/6380147


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