1uwc
From Proteopedia
(Difference between revisions)
| (12 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1uwc.gif|left|200px]]<br /><applet load="1uwc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1uwc, resolution 1.08Å" /> | ||
| - | '''FERULOYL ESTERASE FROM ASPERGILLUS NIGER'''<br /> | ||
| - | == | + | ==Feruloyl esterase from Aspergillus niger== |
| + | <StructureSection load='1uwc' size='340' side='right'caption='[[1uwc]], [[Resolution|resolution]] 1.08Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1uwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UWC FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FER:3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC+ACID'>FER</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1uwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwc OCA], [https://pdbe.org/1uwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uwc RCSB], [https://www.ebi.ac.uk/pdbsum/1uwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAEA_ASPNG FAEA_ASPNG] Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.<ref>PMID:9406381</ref> <ref>PMID:11931668</ref> <ref>PMID:7805053</ref> <ref>PMID:9649839</ref> <ref>PMID:11931668</ref> <ref>PMID:15081808</ref> <ref>PMID:17027758</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/uw/1uwc_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1uwc ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site. | The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site. | ||
| - | + | Structure of a feruloyl esterase from Aspergillus niger.,McAuley KE, Svendsen A, Patkar SA, Wilson KS Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:15103133<ref>PMID:15103133</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1uwc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Aspergillus niger]] | [[Category: Aspergillus niger]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: McAuley KE]] |
| - | + | [[Category: Patkar SA]] | |
| - | [[Category: Patkar | + | [[Category: Svendsen A]] |
| - | [[Category: Svendsen | + | [[Category: Wilson KS]] |
| - | [[Category: Wilson | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Feruloyl esterase from Aspergillus niger
| |||||||||||
