3m83
From Proteopedia
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==Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.12 A resolution (paraoxon inhibitor complex structure)== | ==Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.12 A resolution (paraoxon inhibitor complex structure)== | ||
| - | <StructureSection load='3m83' size='340' side='right' caption='[[3m83]], [[Resolution|resolution]] 2.12Å' scene=''> | + | <StructureSection load='3m83' size='340' side='right'caption='[[3m83]], [[Resolution|resolution]] 2.12Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3m83]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3m83]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M83 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SDP:2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC+ACID'>SDP</scene></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m83 OCA], [https://pdbe.org/3m83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m83 RCSB], [https://www.ebi.ac.uk/pdbsum/3m83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m83 ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m8/3m83_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m8/3m83_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3m83 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3m83" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Acetylxylan esterase|Acetylxylan esterase]] | *[[Acetylxylan esterase|Acetylxylan esterase]] | ||
| + | *[[Acetylxylan esterase 3D structures|Acetylxylan esterase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Axe1]] | ||
| - | [[Category: Hydrolase]] | ||
| - | [[Category: Jcsg]] | ||
| - | [[Category: PSI, Protein structure initiative]] | ||
Current revision
Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.12 A resolution (paraoxon inhibitor complex structure)
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