| Structural highlights
3m83 is a 6 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| NonStd Res: | |
| Related: | 1vlq, 3m81, 3m82 |
| Gene: | TM0077, TM_0077 (ATCC 43589) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CAH_THEMA] Esterase that removes acetyl groups from a number of O-acetylated small substrates, such as acetylated xylose, short xylo-oligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan, 4-methylumbelliferyl acetate or alpha-naphthyl acetate. Able to catalyze rapid hydrolysis of a range of substrates preferably with acetate groups, independent of the alcohol moiety. Exhibits a narrow selectivity for short chain acyl esters (C2-C3). Displays broad substrate specificity by hydrolyzing acetate at 2, 3, and 4 positions of 4-nitrophenyl-beta-D-xylopyranoside (pNP-Xyl) with similar efficiency. Cannot cleave amide linkages.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
TM0077 from Thermotoga maritima is a member of the carbohydrate esterase family 7 and is active on a variety of acetylated compounds, including cephalosporin C. TM0077 esterase activity is confined to short-chain acyl esters (C2-C3), and is optimal around 100 degrees C and pH 7.5. The positional specificity of TM0077 was investigated using 4-nitrophenyl-beta-D-xylopyranoside monoacetates as substrates in a beta-xylosidase-coupled assay. TM0077 hydrolyzes acetate at positions 2, 3, and 4 with equal efficiency. No activity was detected on xylan or acetylated xylan, which implies that TM0077 is an acetyl esterase and not an acetyl xylan esterase as currently annotated. Selenomethionine-substituted and native structures of TM0077 were determined at 2.1 and 2.5 A resolution, respectively, revealing a classic alpha/beta-hydrolase fold. TM0077 assembles into a doughnut-shaped hexamer with small tunnels on either side leading to an inner cavity, which contains the six catalytic centers. Structures of TM0077 with covalently bound phenylmethylsulfonyl fluoride and paraoxon were determined to 2.4 and 2.1 A, respectively, and confirmed that both inhibitors bind covalently to the catalytic serine (Ser188). Upon binding of inhibitor, the catalytic serine adopts an altered conformation, as observed in other esterase and lipases, and supports a previously proposed catalytic mechanism in which Ser hydroxyl rotation prevents reversal of the reaction and allows access of a water molecule for completion of the reaction. Proteins 2012. (c) 2012 Wiley Periodicals, Inc.
Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.,Levisson M, Han GW, Deller MC, Xu Q, Biely P, Hendriks S, Ten Eyck LF, Flensburg C, Roversi P, Miller MD, McMullan D, von Delft F, Kreusch A, Deacon AM, van der Oost J, Lesley SA, Elsliger MA, Kengen SW, Wilson IA Proteins. 2012 Jan 27. doi: 10.1002/prot.24041. PMID:22411095[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Drzewiecki K, Angelov A, Ballschmiter M, Tiefenbach KJ, Sterner R, Liebl W. Hyperthermostable acetyl xylan esterase. Microb Biotechnol. 2010 Jan;3(1):84-92. doi: 10.1111/j.1751-7915.2009.00150.x., Epub 2009 Sep 18. PMID:21255309 doi:http://dx.doi.org/10.1111/j.1751-7915.2009.00150.x
- ↑ Levisson M, Han GW, Deller MC, Xu Q, Biely P, Hendriks S, Ten Eyck LF, Flensburg C, Roversi P, Miller MD, McMullan D, von Delft F, Kreusch A, Deacon AM, van der Oost J, Lesley SA, Elsliger MA, Kengen SW, Wilson IA. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima. Proteins. 2012 Jan 27. doi: 10.1002/prot.24041. PMID:22411095 doi:10.1002/prot.24041
- ↑ Hedge MK, Gehring AM, Adkins CT, Weston LA, Lavis LD, Johnson RJ. The structural basis for the narrow substrate specificity of an acetyl esterase from Thermotoga maritima. Biochim Biophys Acta. 2012 Sep;1824(9):1024-30. doi:, 10.1016/j.bbapap.2012.05.009. Epub 2012 Jun 1. PMID:22659119 doi:http://dx.doi.org/10.1016/j.bbapap.2012.05.009
- ↑ Levisson M, Han GW, Deller MC, Xu Q, Biely P, Hendriks S, Ten Eyck LF, Flensburg C, Roversi P, Miller MD, McMullan D, von Delft F, Kreusch A, Deacon AM, van der Oost J, Lesley SA, Elsliger MA, Kengen SW, Wilson IA. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima. Proteins. 2012 Jan 27. doi: 10.1002/prot.24041. PMID:22411095 doi:10.1002/prot.24041
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