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1vlq
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vlq]] is a 12 chain structure 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VLQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1vlq]] is a 12 chain structure 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VLQ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><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=2336 Thermotoga maritima])</td></tr> | + | <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=2336 Thermotoga maritima])</td></tr> |
| - | <tr><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='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><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://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://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> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q9WXT2_THEMA Q9WXT2_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:22659119</ref> <ref>PMID:22411095</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Cephalosporin-C deacetylase]] | [[Category: Cephalosporin-C deacetylase]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: | + | [[Category: Structural genomic]] |
[[Category: Acetyl xylan esterase]] | [[Category: Acetyl xylan esterase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Jcsg]] | [[Category: Jcsg]] | ||
| - | [[Category: | + | [[Category: PSI, Protein structure initiative]] |
| - | + | ||
| - | + | ||
| - | + | ||
[[Category: Tm0077]] | [[Category: Tm0077]] | ||
Revision as of 02:41, 25 December 2014
Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution
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