2qub: Difference between revisions

==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 [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>, <scene name='pdbsite=AC8:Ca+Binding+Site+For+Residue+A+621'>AC8</scene>, <scene name='pdbsite=AC9:Ca+Binding+Site+For+Residue+C+614'>AC9</scene>, <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+C+615'>BC1</scene>, <scene name='pdbsite=BC2:Ca+Binding+Site+For+Residue+C+616'>BC2</scene>, <scene name='pdbsite=BC3:Ca+Binding+Site+For+Residue+C+617'>BC3</scene>, <scene name='pdbsite=BC4:Ca+Binding+Site+For+Residue+C+618'>BC4</scene>, <scene name='pdbsite=BC5:Ca+Binding+Site+For+Residue+C+619'>BC5</scene>, <scene name='pdbsite=BC6:Ca+Binding+Site+For+Residue+C+620'>BC6</scene>, <scene name='pdbsite=BC7:Ca+Binding+Site+For+Residue+C+621'>BC7</scene>, <scene name='pdbsite=BC8:Ca+Binding+Site+For+Residue+E+614'>BC8</scene>, <scene name='pdbsite=BC9:Ca+Binding+Site+For+Residue+E+615'>BC9</scene>, <scene name='pdbsite=CC1:Ca+Binding+Site+For+Residue+E+616'>CC1</scene>, <scene name='pdbsite=CC2:Ca+Binding+Site+For+Residue+E+617'>CC2</scene>, <scene name='pdbsite=CC3:Ca+Binding+Site+For+Residue+E+618'>CC3</scene>, <scene name='pdbsite=CC4:Ca+Binding+Site+For+Residue+E+619'>CC4</scene>, <scene name='pdbsite=CC5:Ca+Binding+Site+For+Residue+E+620'>CC5</scene>, <scene name='pdbsite=CC6:Ca+Binding+Site+For+Residue+E+621'>CC6</scene>, <scene name='pdbsite=CC7:Ca+Binding+Site+For+Residue+G+614'>CC7</scene>, <scene name='pdbsite=CC8:Ca+Binding+Site+For+Residue+G+615'>CC8</scene>, <scene name='pdbsite=CC9:Ca+Binding+Site+For+Residue+G+616'>CC9</scene>, <scene name='pdbsite=DC1:Ca+Binding+Site+For+Residue+G+617'>DC1</scene>, <scene name='pdbsite=DC2:Ca+Binding+Site+For+Residue+G+618'>DC2</scene>, <scene name='pdbsite=DC3:Ca+Binding+Site+For+Residue+G+619'>DC3</scene>, <scene name='pdbsite=DC4:Ca+Binding+Site+For+Residue+G+620'>DC4</scene>, <scene name='pdbsite=DC5:Ca+Binding+Site+For+Residue+G+621'>DC5</scene>, <scene name='pdbsite=DC6:Ca+Binding+Site+For+Residue+I+614'>DC6</scene>, <scene name='pdbsite=DC7:Ca+Binding+Site+For+Residue+I+615'>DC7</scene>, <scene name='pdbsite=DC8:Ca+Binding+Site+For+Residue+I+616'>DC8</scene>, <scene name='pdbsite=DC9:Ca+Binding+Site+For+Residue+I+617'>DC9</scene>, <scene name='pdbsite=EC1:Ca+Binding+Site+For+Residue+I+618'>EC1</scene>, <scene name='pdbsite=EC2:Ca+Binding+Site+For+Residue+I+619'>EC2</scene>, <scene name='pdbsite=EC3:Ca+Binding+Site+For+Residue+I+620'>EC3</scene>, <scene name='pdbsite=EC4:Ca+Binding+Site+For+Residue+I+621'>EC4</scene>, <scene name='pdbsite=EC5:Ca+Binding+Site+For+Residue+K+614'>EC5</scene>, <scene name='pdbsite=EC6:Ca+Binding+Site+For+Residue+K+615'>EC6</scene>, <scene name='pdbsite=EC7:Ca+Binding+Site+For+Residue+K+616'>EC7</scene>, <scene name='pdbsite=EC8:Ca+Binding+Site+For+Residue+K+617'>EC8</scene>, <scene name='pdbsite=EC9:Ca+Binding+Site+For+Residue+K+618'>EC9</scene>, <scene name='pdbsite=FC1:Ca+Binding+Site+For+Residue+K+619'>FC1</scene>, <scene name='pdbsite=FC2:Ca+Binding+Site+For+Residue+K+620'>FC2</scene> and <scene name='pdbsite=FC3:Ca+Binding+Site+For+Residue+K+621'>FC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUB OCA].

 

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: Baumann, U.]]

[[Category: Meier, R.]]

[[Category: CA]]