2czq: Difference between revisions
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==A novel cutinase-like protein from Cryptococcus sp.== | ==A novel cutinase-like protein from Cryptococcus sp.== | ||
<StructureSection load='2czq' size='340' side='right' caption='[[2czq]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='2czq' size='340' side='right'caption='[[2czq]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2czq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptococcus_sp. Cryptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CZQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2czq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptococcus_sp. Cryptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CZQ FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cryptococcus sp]] | [[Category: Cryptococcus sp]] | ||
[[Category: Large Structures]] | |||
[[Category: Iefuji, H]] | [[Category: Iefuji, H]] | ||
[[Category: Ikeda, H]] | [[Category: Ikeda, H]] |
Revision as of 10:54, 4 March 2020
A novel cutinase-like protein from Cryptococcus sp.A novel cutinase-like protein from Cryptococcus sp.
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity. Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2.,Kodama Y, Masaki K, Kondo H, Suzuki M, Tsuda S, Nagura T, Shimba N, Suzuki E, Iefuji H Proteins. 2009 Nov 15;77(3):710-7. PMID:19544571[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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