2qua
From Proteopedia
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|PDB= 2qua |SIZE=350|CAPTION= <scene name='initialview01'>2qua</scene>, resolution 1.95Å | |PDB= 2qua |SIZE=350|CAPTION= <scene name='initialview01'>2qua</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Residue+A+614'>AC1</scene>, <scene name='pdbsite=AC2:Ca+Binding+Site+For+Residue+A+615'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Residue+A+616'>AC3</scene>, <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+A+617'>AC4</scene>, <scene name='pdbsite=AC5:Ca+Binding+Site+For+Residue+A+618'>AC5</scene>, <scene name='pdbsite=AC6:Ca+Binding+Site+For+Residue+A+619'>AC6</scene>, <scene name='pdbsite=AC7:Ca+Binding+Site+For+Residue+A+620'>AC7</scene> and <scene name='pdbsite=AC8:Ca+Binding+Site+For+Residue+A+621'>AC8</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Residue+A+614'>AC1</scene>, <scene name='pdbsite=AC2:Ca+Binding+Site+For+Residue+A+615'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Residue+A+616'>AC3</scene>, <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+A+617'>AC4</scene>, <scene name='pdbsite=AC5:Ca+Binding+Site+For+Residue+A+618'>AC5</scene>, <scene name='pdbsite=AC6:Ca+Binding+Site+For+Residue+A+619'>AC6</scene>, <scene name='pdbsite=AC7:Ca+Binding+Site+For+Residue+A+620'>AC7</scene> and <scene name='pdbsite=AC8:Ca+Binding+Site+For+Residue+A+621'>AC8</scene> | ||
| - | |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=[[2qub|2QUB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qua OCA], [http://www.ebi.ac.uk/pdbsum/2qua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qua 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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:24 2008'' |
Revision as of 01:53, 31 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | lipA (Serratia marcescens) | ||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Related: | 2QUB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of 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
2QUA 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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