2qua
From Proteopedia
(New page: 200px<br /><applet load="2qua" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qua, resolution 1.95Å" /> '''Crystal structure of...) |
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caption="2qua, resolution 1.95Å" /> | caption="2qua, resolution 1.95Å" /> | ||
'''Crystal structure of LipA from Serratia marcescens'''<br /> | '''Crystal structure of LipA from Serratia marcescens'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
| - | 2QUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUA OCA]. | + | 2QUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUA OCA]. |
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| + | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17728256 17728256] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[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 Thu Jan 31 10:59:45 2008'' |
Revision as of 08:59, 31 January 2008
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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 with as ligand. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Known structural/functional Sites: , , , , , , and . 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
Page seeded by OCA on Thu Jan 31 10:59:45 2008
