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| | <StructureSection load='1g66' size='340' side='right'caption='[[1g66]], [[Resolution|resolution]] 0.90Å' scene=''> | | <StructureSection load='1g66' size='340' side='right'caption='[[1g66]], [[Resolution|resolution]] 0.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g66]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Penicillium_purpurogenum Penicillium purpurogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G66 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g66]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Talaromyces_purpureogenus Talaromyces purpureogenus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G66 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bs9|1bs9]], [[2axe|2axe]]</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=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylesterase Acetylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.6 3.1.1.6] </span></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=1g66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g66 OCA], [https://pdbe.org/1g66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g66 RCSB], [https://www.ebi.ac.uk/pdbsum/1g66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g66 ProSAT]</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=1g66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g66 OCA], [http://pdbe.org/1g66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g66 RCSB], [http://www.ebi.ac.uk/pdbsum/1g66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g66 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AXE2_PENPU AXE2_PENPU]] Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.<ref>PMID:8756392</ref> | + | [https://www.uniprot.org/uniprot/AXE2_TALPU AXE2_TALPU] Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.<ref>PMID:8756392</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/1g66_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/1g66_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acetylesterase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Penicillium purpurogenum]] | + | [[Category: Talaromyces purpureogenus]] |
| - | [[Category: Erman, M]] | + | [[Category: Erman M]] |
| - | [[Category: Eyzaguirre, J]] | + | [[Category: Eyzaguirre J]] |
| - | [[Category: Ghosh, D]] | + | [[Category: Ghosh D]] |
| - | [[Category: Gutierrez, R]] | + | [[Category: Gutierrez R]] |
| - | [[Category: Jornvall, H]] | + | [[Category: Jornvall H]] |
| - | [[Category: Lala, P]] | + | [[Category: Lala P]] |
| - | [[Category: Pangborn, W]] | + | [[Category: Pangborn W]] |
| - | [[Category: Sawicki, M]] | + | [[Category: Sawicki M]] |
| - | [[Category: Thiel, D J]] | + | [[Category: Thiel DJ]] |
| - | [[Category: Acetyl xylopyranose]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine hydrolase]]
| + | |
| - | [[Category: Xylan]]
| + | |
| Structural highlights
Function
AXE2_TALPU Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.[1]
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
Acetylxylan esterase (AXEII; 207 amino acids) from Penicillium purpurogenum has substrate specificities toward acetate esters of d-xylopyranose residues in xylan and belongs to a new class of alpha/beta hydrolases. The crystal structure of AXEII has been determined by single isomorphous replacement and anomalous scattering, and refined at 0.90- and 1.10-A resolutions with data collected at 85 K and 295 K, respectively. The tertiary structure consists of a doubly wound alpha/beta sandwich, having a central six-stranded parallel beta-sheet flanked by two parallel alpha-helices on each side. The catalytic residues Ser(90), His(187), and Asp(175) are located at the C-terminal end of the sheet, an exposed region of the molecule. The serine and histidine side chains in the 295 K structure show the frequently observed conformations in which Ser(90) is trans and the hydroxyl group is in the plane of the imidazole ring of His(187). However, the structure at 85 K displays an additional conformation in which Ser(90) side-chain hydroxyl is away from the plane of the imidazole ring of His(187). The His(187) side chain forms a hydrogen bond with a sulfate ion and adopts an altered conformation. The only other known hydrolase that has a similar tertiary structure is Fusarium solani cutinase. The exposed nature of the catalytic triad suggests that AXEII is a pure esterase, i.e. an alpha/beta hydrolase with specificity for nonlipidic polar substrates.
Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A.,Ghosh D, Sawicki M, Lala P, Erman M, Pangborn W, Eyzaguirre J, Gutierrez R, Jornvall H, Thiel DJ J Biol Chem. 2001 Apr 6;276(14):11159-66. Epub 2000 Dec 29. PMID:11134051[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Egana L, Gutierrez R, Caputo V, Peirano A, Steiner J, Eyzaguirre J. Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum. Biotechnol Appl Biochem. 1996 Aug;24 ( Pt 1):33-9. PMID:8756392
- ↑ Ghosh D, Sawicki M, Lala P, Erman M, Pangborn W, Eyzaguirre J, Gutierrez R, Jornvall H, Thiel DJ. Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A. J Biol Chem. 2001 Apr 6;276(14):11159-66. Epub 2000 Dec 29. PMID:11134051 doi:10.1074/jbc.M008831200
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