Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15
GDSL esterase J15 (EstJ15) is a member of Family II of lipolytic enzyme. The enzyme was further classified in subgroup SGNH hydrolase due to the presence of highly conserve motif, Ser-Gly-Asn-His in four conserved blocks I, II, III, and V, respectively. X-ray quality crystal of EstJ15 was obtained f...
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| Format: | Article |
| Language: | English |
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Elsevier
2018
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| Online Access: | http://psasir.upm.edu.my/id/eprint/72151/ http://psasir.upm.edu.my/id/eprint/72151/1/Crystallization%20and%20structure%20elucidation%20of%20GDSL%20esterase%20of%20Photobacterium%20sp.%20J15.pdf |
| _version_ | 1848857050980810752 |
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| author | Syed Mazlan, Sharifah Nur Hidayah Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha Sabri, Suriana Jonet, Mohd Anuar Leow, Adam Thean Chor |
| author_facet | Syed Mazlan, Sharifah Nur Hidayah Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha Sabri, Suriana Jonet, Mohd Anuar Leow, Adam Thean Chor |
| author_sort | Syed Mazlan, Sharifah Nur Hidayah |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | GDSL esterase J15 (EstJ15) is a member of Family II of lipolytic enzyme. The enzyme was further classified in subgroup SGNH hydrolase due to the presence of highly conserve motif, Ser-Gly-Asn-His in four conserved blocks I, II, III, and V, respectively. X-ray quality crystal of EstJ15 was obtained from optimized formulation containing 0.10 M ammonium sulphate, 0.15 M sodium cacodylate trihydrate pH 6.5, and 20% PEG 8000. The crystal structure of EstJ15 was solved at 1.38 Å with one molecule per asymmetric unit. The structure exhibits α/β hydrolase fold and shared low amino acid sequence identity of 23% with the passenger domain of the autotransporter EstA of Pseudomonas aeruginosa. The active site is located at the centre of the structure, formed a narrow tunnel that hinder long substrates to be catalysed which was proven by the protein-ligand docking analysis. This study facilitates the understanding of high substrate specificity of EstJ15 and provide insights on its catalytic mechanism. |
| first_indexed | 2025-11-15T11:51:24Z |
| format | Article |
| id | upm-72151 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T11:51:24Z |
| publishDate | 2018 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-721512020-03-04T08:05:37Z http://psasir.upm.edu.my/id/eprint/72151/ Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 Syed Mazlan, Sharifah Nur Hidayah Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha Sabri, Suriana Jonet, Mohd Anuar Leow, Adam Thean Chor GDSL esterase J15 (EstJ15) is a member of Family II of lipolytic enzyme. The enzyme was further classified in subgroup SGNH hydrolase due to the presence of highly conserve motif, Ser-Gly-Asn-His in four conserved blocks I, II, III, and V, respectively. X-ray quality crystal of EstJ15 was obtained from optimized formulation containing 0.10 M ammonium sulphate, 0.15 M sodium cacodylate trihydrate pH 6.5, and 20% PEG 8000. The crystal structure of EstJ15 was solved at 1.38 Å with one molecule per asymmetric unit. The structure exhibits α/β hydrolase fold and shared low amino acid sequence identity of 23% with the passenger domain of the autotransporter EstA of Pseudomonas aeruginosa. The active site is located at the centre of the structure, formed a narrow tunnel that hinder long substrates to be catalysed which was proven by the protein-ligand docking analysis. This study facilitates the understanding of high substrate specificity of EstJ15 and provide insights on its catalytic mechanism. Elsevier 2018-11 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/72151/1/Crystallization%20and%20structure%20elucidation%20of%20GDSL%20esterase%20of%20Photobacterium%20sp.%20J15.pdf Syed Mazlan, Sharifah Nur Hidayah and Mohamad Ali, Mohd Shukuri and Raja Abdul Rahman, Raja Noor Zaliha and Sabri, Suriana and Jonet, Mohd Anuar and Leow, Adam Thean Chor (2018) Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15. International Journal of Biological Macromolecules, 119. 1188 - 1194. ISSN 0141-8130; ESSN: 1879-0003 https://www.sciencedirect.com/science/article/pii/S014181301832840X 10.1016/j.ijbiomac.2018.08.022 |
| spellingShingle | Syed Mazlan, Sharifah Nur Hidayah Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha Sabri, Suriana Jonet, Mohd Anuar Leow, Adam Thean Chor Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 |
| title | Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 |
| title_full | Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 |
| title_fullStr | Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 |
| title_full_unstemmed | Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 |
| title_short | Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 |
| title_sort | crystallization and structure elucidation of gdsl esterase of photobacterium sp. j15 |
| url | http://psasir.upm.edu.my/id/eprint/72151/ http://psasir.upm.edu.my/id/eprint/72151/ http://psasir.upm.edu.my/id/eprint/72151/ http://psasir.upm.edu.my/id/eprint/72151/1/Crystallization%20and%20structure%20elucidation%20of%20GDSL%20esterase%20of%20Photobacterium%20sp.%20J15.pdf |