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| | {{STRUCTURE_2qua| PDB=2qua | SCENE= }} | | {{STRUCTURE_2qua| PDB=2qua | SCENE= }} |
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| - | '''Crystal structure of LipA from Serratia marcescens'''
| + | ===Crystal structure of LipA from Serratia marcescens=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17728256}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17728256 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17728256}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta roll]] | | [[Category: Beta roll]] |
| | [[Category: Helical hairpin]] | | [[Category: Helical hairpin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:42:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:27:13 2008'' |
Revision as of 23:27, 27 July 2008
Template:STRUCTURE 2qua
Crystal structure of LipA from Serratia marcescens
Template:ABSTRACT PUBMED 17728256
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
Page seeded by OCA on Mon Jul 28 02:27:13 2008
