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4kry

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Template:STRUCTURE 4kry

Contents

Structure of Aes from E. coli in covalent complex with PMS

Template:ABSTRACT PUBMED 23934774

Function

[AES_ECOLI] Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity.[1] [2] [3]

About this Structure

4kry is a 6 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA.

Reference

  • Schiefner A, Gerber K, Brosig A, Boos W. Structural and mutational analyses of Aes, an inhibitor of MalT in Escherichia coli. Proteins. 2013 Aug 12. doi: 10.1002/prot.24383. PMID:23934774 doi:10.1002/prot.24383
  1. ↑ Kanaya S, Koyanagi T, Kanaya E. An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase. Biochem J. 1998 May 15;332 ( Pt 1):75-80. PMID:9576853
  2. ↑ Joly N, Danot O, Schlegel A, Boos W, Richet E. The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J Biol Chem. 2002 May 10;277(19):16606-13. Epub 2002 Feb 26. PMID:11867639 doi:http://dx.doi.org/10.1074/jbc.M200991200
  3. ↑ Mandrich L, Caputo E, Martin BM, Rossi M, Manco G. The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism. J Biol Chem. 2002 Dec 13;277(50):48241-7. Epub 2002 Oct 8. PMID:12374803 doi:http://dx.doi.org/10.1074/jbc.M207398200

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