1i6w
From Proteopedia
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|PDB= 1i6w |SIZE=350|CAPTION= <scene name='initialview01'>1i6w</scene>, resolution 1.5Å | |PDB= 1i6w |SIZE=350|CAPTION= <scene name='initialview01'>1i6w</scene>, resolution 1.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span> |
|GENE= LIPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= LIPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6w OCA], [http://www.ebi.ac.uk/pdbsum/1i6w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i6w RCSB]</span> | ||
}} | }} | ||
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[[Category: Jaeger, K E.]] | [[Category: Jaeger, K E.]] | ||
[[Category: Pouderoyen, G van.]] | [[Category: Pouderoyen, G van.]] | ||
| - | [[Category: CD]] | ||
[[Category: alpha/beta hydrolase]] | [[Category: alpha/beta hydrolase]] | ||
| - | ''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 21:15:26 2008'' |
Revision as of 18:15, 30 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | LIPA (Bacillus subtilis) | ||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE: A MINIMAL ALPHA/BETA HYDROLASE ENZYME
Overview
The X-ray structure of the lipase LipA from Bacillus subtilis has been determined at 1.5 A resolution. It is the first structure of a member of homology family 1.4 of bacterial lipases. The lipase shows a compact minimal alpha/beta hydrolase fold with a six-stranded parallel beta-sheet flanked by five alpha-helices, two on one side of the sheet and three on the other side. The catalytic triad residues, Ser77, Asp133 and His156, and the residues forming the oxyanion hole (backbone amide groups of Ile12 and Met78) are in positions very similar to those of other lipases of known structure. However, no lid domain is present and the active-site nucleophile Ser77 is solvent-exposed. A model of substrate binding is proposed on the basis of a comparison with other lipases with a covalently bound tetrahedral intermediate mimic. It explains the preference of the enzyme for substrates with C8 fatty acid chains.
About this Structure
1I6W is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme., van Pouderoyen G, Eggert T, Jaeger KE, Dijkstra BW, J Mol Biol. 2001 May 25;309(1):215-26. PMID:11491291
Page seeded by OCA on Sun Mar 30 21:15:26 2008
