1jji: Difference between revisions
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|PDB= 1jji |SIZE=350|CAPTION= <scene name='initialview01'>1jji</scene>, resolution 2.20Å | |PDB= 1jji |SIZE=350|CAPTION= <scene name='initialview01'>1jji</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | |LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jji OCA], [http://www.ebi.ac.uk/pdbsum/1jji PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jji RCSB]</span> | |||
}} | }} | ||
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[[Category: Simone, G De.]] | [[Category: Simone, G De.]] | ||
[[Category: Sorrentino, N.]] | [[Category: Sorrentino, N.]] | ||
[[Category: alpha-beta hydrolase fold]] | [[Category: alpha-beta hydrolase fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:34:35 2008'' | ||
Revision as of 21:34, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Activity: | Carboxylesterase, with EC number 3.1.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure of a Hyper-thermophilic Carboxylesterase from the Archaeon Archaeoglobus fulgidus
OverviewOverview
The crystal structure of AFEST, a novel hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus, complexed with a sulphonyl derivative, has been determined and refined to 2.2 A resolution. This enzyme, which has recently been classified as a member of the hormone- sensitive-lipase (H) group of the esterase/lipase superfamily, presents a canonical alpha/beta hydrolase core, shielded on the C-terminal side by a cap region composed of five alpha-helices. It contains the catalytic triad Ser160, His285 and Asp255, whereby the nucleophile is covalently modified and the oxyanion hole formed by Gly88, Gly89 and Ala161. A structural comparison of AFEST with its mesophilic and thermophilic homologues, Brefeldin A esterase from Bacillus subtilis (BFAE) and EST2 from Alicyclobacillus acidocaldarius, reveals an increase in the number of intramolecular ion pairs and secondary structure content, as well as a significant reduction in loop extensions and ratio of hydrophobic to charged surface area. The variety of structural differences suggests possible strategies for thermostabilization of lipases and esterases with potential industrial applications.
About this StructureAbout this Structure
1JJI is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus., De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C, J Mol Biol. 2001 Nov 30;314(3):507-18. PMID:11846563
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