4kry
From Proteopedia
(Difference between revisions)
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===Structure of Aes from E. coli in covalent complex with PMS=== | ===Structure of Aes from E. coli in covalent complex with PMS=== | ||
{{ABSTRACT_PUBMED_23934774}} | {{ABSTRACT_PUBMED_23934774}} | ||
+ | |||
+ | ==Function== | ||
+ | [[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== | ||
- | [[4kry]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4kry]] is a 6 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=4KRY OCA]. |
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:023934774</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:023934774</ref><references group="xtra"/><references/> | ||
- | [[Category: | + | [[Category: Ecoli]] |
[[Category: Boos, W.]] | [[Category: Boos, W.]] | ||
[[Category: Brosig, A.]] | [[Category: Brosig, A.]] |
Revision as of 09:10, 5 February 2014
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
- ↑ 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
- ↑ 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
- ↑ 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