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1vlq

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Revision as of 07:13, 4 April 2018

Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution

Structural highlights

1vlq is a 12 chain structure with sequence from Thema. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	TM0077 (THEMA)
Activity:	Cephalosporin-C deacetylase, with EC number 3.1.1.41
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vlq"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution==
 <StructureSection load='1vlq' size='340' side='right' caption='[[1vlq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0077 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cephalosporin-C_deacetylase Cephalosporin-C deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.41 3.1.1.41] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlq OCA], [http://pdbe.org/1vlq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vlq RCSB], [http://www.ebi.ac.uk/pdbsum/1vlq PDBsum], [http://www.topsan.org/Proteins/JCSG/1vlq TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlq OCA], [http://pdbe.org/1vlq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vlq RCSB], [http://www.ebi.ac.uk/pdbsum/1vlq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlq ProSAT], [http://www.topsan.org/Proteins/JCSG/1vlq TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vl/1vlq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vl/1vlq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1vlq

From Proteopedia

Revision as of 07:13, 4 April 2018

Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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