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Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15

Overview of attention for article published in International Journal of Biological Macromolecules, August 2018
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  • Above-average Attention Score compared to outputs of the same age and source (57th percentile)

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Title
Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15
Published in
International Journal of Biological Macromolecules, August 2018
DOI 10.1016/j.ijbiomac.2018.08.022
Pubmed ID
Authors

Sharifah Nur Hidayah Syed Mazlan, Mohd Shukuri Mohamad Ali, Raja Noor Zaliha Raja Abd Rahman, Suriana Sabri, Mohd Anuar Jonet, Thean Chor Leow

Abstract

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.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 19 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 19 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 4 21%
Student > Ph. D. Student 4 21%
Researcher 3 16%
Student > Postgraduate 2 11%
Student > Master 1 5%
Other 1 5%
Unknown 4 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 42%
Agricultural and Biological Sciences 2 11%
Engineering 2 11%
Chemistry 1 5%
Physics and Astronomy 1 5%
Other 0 0%
Unknown 5 26%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 August 2018.
All research outputs
#19,954,338
of 25,385,509 outputs
Outputs from International Journal of Biological Macromolecules
#4,167
of 7,501 outputs
Outputs of similar age
#249,650
of 341,333 outputs
Outputs of similar age from International Journal of Biological Macromolecules
#68
of 191 outputs
Altmetric has tracked 25,385,509 research outputs across all sources so far. This one is in the 18th percentile – i.e., 18% of other outputs scored the same or lower than it.
So far Altmetric has tracked 7,501 research outputs from this source. They receive a mean Attention Score of 2.9. This one is in the 40th percentile – i.e., 40% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 341,333 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 22nd percentile – i.e., 22% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 191 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 57% of its contemporaries.