1g66: Difference between revisions
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==ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION== | |||
<StructureSection load='1g66' size='340' side='right'caption='[[1g66]], [[Resolution|resolution]] 0.90Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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='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> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[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/g6/1g66_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=1g66 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:11134051</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1g66" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Acetylxylan esterase|Acetylxylan esterase]] | *[[Acetylxylan esterase 3D structures|Acetylxylan esterase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Erman | [[Category: Talaromyces purpureogenus]] | ||
[[Category: Eyzaguirre | [[Category: Erman M]] | ||
[[Category: Ghosh | [[Category: Eyzaguirre J]] | ||
[[Category: Gutierrez | [[Category: Ghosh D]] | ||
[[Category: Jornvall | [[Category: Gutierrez R]] | ||
[[Category: Lala | [[Category: Jornvall H]] | ||
[[Category: Pangborn | [[Category: Lala P]] | ||
[[Category: Sawicki | [[Category: Pangborn W]] | ||
[[Category: Thiel | [[Category: Sawicki M]] | ||
[[Category: Thiel DJ]] | |||
