2qub

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|PDB= 2qub |SIZE=350|CAPTION= <scene name='initialview01'>2qub</scene>, resolution 1.80&Aring;
|PDB= 2qub |SIZE=350|CAPTION= <scene name='initialview01'>2qub</scene>, resolution 1.80&Aring;
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-
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
+
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=615 Serratia marcescens])
|GENE= lipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=615 Serratia marcescens])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2qua|2QUA]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qub OCA], [http://www.ebi.ac.uk/pdbsum/2qub PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qub RCSB]</span>
}}
}}
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[[Category: Baumann, U.]]
[[Category: Baumann, U.]]
[[Category: Meier, R.]]
[[Category: Meier, R.]]
-
[[Category: CA]]
 
[[Category: alpha/beta hydrolase]]
[[Category: alpha/beta hydrolase]]
[[Category: beta roll]]
[[Category: beta roll]]
[[Category: helical hairpin]]
[[Category: helical hairpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:29:40 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:23 2008''

Revision as of 01:53, 31 March 2008


PDB ID 2qub

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites: , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and
Ligands:
Gene: lipA (Serratia marcescens)
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Related: 2QUA


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of extracellular lipase LipA from Serratia marcescens


Overview

Lipase LipA from Serratia marcescens is a 613-amino acid enzyme belonging to family I.3 of lipolytic enzymes that has an important biotechnological application in the production of a chiral precursor for the coronary vasodilator diltiazem. Like other family I.3 lipases, LipA is secreted by Gram-negative bacteria via a type I secretion system and possesses 13 copies of a calcium binding tandem repeat motif, GGXGXDXUX (U, hydrophobic amino acids), in the C-terminal part of the polypeptide chain. The 1.8-A crystal structure of LipA reveals a close relation to eukaryotic lipases, whereas family I.1 and I.2 enzymes appear to be more distantly related. Interestingly, the structure shows for the N-terminal lipase domain a variation on the canonical alpha/beta hydrolase fold in an open conformation, where the putative lid helix is anchored by a Ca(2+) ion essential for activity. Another novel feature observed in this lipase structure is the presence of a helical hairpin additional to the putative lid helix that exposes a hydrophobic surface to the aqueous medium and might function as an additional lid. The tandem repeats form two separated parallel beta-roll domains that pack tightly against each other. Variations of the consensus sequence of the tandem repeats within the second beta-roll result in an asymmetric Ca(2+) binding on only one side of the roll. The analysis of the properties of the beta-roll domains suggests an intramolecular chaperone function.

About this Structure

2QUB is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens., Meier R, Drepper T, Svensson V, Jaeger KE, Baumann U, J Biol Chem. 2007 Oct 26;282(43):31477-83. Epub 2007 Aug 28. PMID:17728256

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