1vlq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1vlq" [edit=sysop:move=sysop])
Current revision (07:34, 30 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1vlq.png|left|200px]]
 
-
<!--
+
==Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution==
-
The line below this paragraph, containing "STRUCTURE_1vlq", creates the "Structure Box" on the page.
+
<StructureSection load='1vlq' size='340' side='right'caption='[[1vlq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1vlq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLQ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
{{STRUCTURE_1vlq| PDB=1vlq | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlq OCA], [https://pdbe.org/1vlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlq RCSB], [https://www.ebi.ac.uk/pdbsum/1vlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlq ProSAT], [https://www.topsan.org/Proteins/JCSG/1vlq TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CAH_THEMA 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.<ref>PMID:21255309</ref> <ref>PMID:22411095</ref> <ref>PMID:22659119</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<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/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vlq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution===
+
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<ref>PMID:22411095</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_22411095}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1vlq" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 22411095 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_22411095}}
+
-
 
+
-
==About this Structure==
+
-
[[1vlq]] is a 12 chain structure of [[Acetylxylan esterase]] with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLQ OCA].
+
==See Also==
==See Also==
-
*[[Acetylxylan esterase|Acetylxylan esterase]]
+
*[[Acetylxylan esterase 3D structures|Acetylxylan esterase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:022411095</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Cephalosporin-C deacetylase]]
+
</StructureSection>
-
[[Category: Thermotoga maritima]]
+
[[Category: Large Structures]]
-
[[Category: JCSG, Joint Center for Structural Genomics.]]
+
[[Category: Thermotoga maritima MSB8]]
-
[[Category: Acetyl xylan esterase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Jcsg]]
+
-
[[Category: Joint center for structural genomic]]
+
-
[[Category: Protein structure initiative]]
+
-
[[Category: Psi]]
+
-
[[Category: Structural genomic]]
+
-
[[Category: Tm0077]]
+

Current revision

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

PDB ID 1vlq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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