4krx

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===Structure of Aes from E. coli===
===Structure of Aes from E. coli===
{{ABSTRACT_PUBMED_23934774}}
{{ABSTRACT_PUBMED_23934774}}
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==Function==
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[[http://www.uniprot.org/uniprot/AES_ECOLI 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.<ref>PMID:9576853</ref> <ref>PMID:11867639</ref> <ref>PMID:12374803</ref>
==About this Structure==
==About this Structure==
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[[4krx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRX OCA].
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[[4krx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRX OCA].
==Reference==
==Reference==
<ref group="xtra">PMID:023934774</ref><references group="xtra"/><references/>
<ref group="xtra">PMID:023934774</ref><references group="xtra"/><references/>
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[[Category: Escherichia coli k-12]]
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[[Category: Ecoli]]
[[Category: Boos, W.]]
[[Category: Boos, W.]]
[[Category: Brosig, A.]]
[[Category: Brosig, A.]]

Revision as of 09:19, 5 February 2014

Template:STRUCTURE 4krx

Contents

Structure of Aes from E. coli

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

4krx is a 3 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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