1bs9: Difference between revisions

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[[Image:1bs9.jpg|left|200px]]
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{{STRUCTURE_1bs9|  PDB=1bs9  |  SCENE=  }}
'''ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS'''


==ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS==
<StructureSection load='1bs9' size='340' side='right'caption='[[1bs9]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bs9]] 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=1BS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BS9 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]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1bs9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bs9 OCA], [https://pdbe.org/1bs9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bs9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bs9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bs9 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/bs/1bs9_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=1bs9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymatic and non-enzymatic iodination of the amino acid tyrosine is a well known phenomenon. The iodination technique has been widely used for labeling proteins. Using high-resolution X-ray crystallographic techniques, the chemical and three-dimensional structures of iodotyrosines formed by non-enzymatic incorporation of I atoms into tyrosine residues of a crystalline protein are described. Acetylxylan esterase (AXE II; 207 amino-acid residues) from Penicillium purpurogenum has substrate specificities towards acetate esters of D-xylopyranose residues in xylan and belongs to a new class of alpha/beta hydrolases. The crystals of the enzyme are highly ordered, tightly packed and diffract to better than sub-angstrom resolution at 85 K. The iodination technique has been utilized to prepare an isomorphous derivative of the AXE II crystal. The structure of the enzyme determined at 1.10 A resolution exclusively by normal and anomalous scattering from I atoms, along with the structure of the iodinated complex at 1.80 A resolution, demonstrate the formation of covalent bonds between I atoms and C atoms at ortho positions to the hydroxyl groups of two tyrosyl moieties, yielding iodotyrosines.


==Overview==
Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase.,Ghosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jornvall H, Gutierrez R, Eyzaguirre J Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):779-84. PMID:10089308<ref>PMID:10089308</ref>
Enzymatic and non-enzymatic iodination of the amino acid tyrosine is a well known phenomenon. The iodination technique has been widely used for labeling proteins. Using high-resolution X-ray crystallographic techniques, the chemical and three-dimensional structures of iodotyrosines formed by non-enzymatic incorporation of I atoms into tyrosine residues of a crystalline protein are described. Acetylxylan esterase (AXE II; 207 amino-acid residues) from Penicillium purpurogenum has substrate specificities towards acetate esters of D-xylopyranose residues in xylan and belongs to a new class of alpha/beta hydrolases. The crystals of the enzyme are highly ordered, tightly packed and diffract to better than sub-angstrom resolution at 85 K. The iodination technique has been utilized to prepare an isomorphous derivative of the AXE II crystal. The structure of the enzyme determined at 1.10 A resolution exclusively by normal and anomalous scattering from I atoms, along with the structure of the iodinated complex at 1.80 A resolution, demonstrate the formation of covalent bonds between I atoms and C atoms at ortho positions to the hydroxyl groups of two tyrosyl moieties, yielding iodotyrosines.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BS9 is a [[Single protein]] structure of 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=1BS9 OCA].
</div>
<div class="pdbe-citations 1bs9" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase., Ghosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jornvall H, Gutierrez R, Eyzaguirre J, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):779-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089308 10089308]
*[[Acetylxylan esterase 3D structures|Acetylxylan esterase 3D structures]]
[[Category: Acetylesterase]]
== References ==
[[Category: Penicillium purpurogenum]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Erman, M.]]
</StructureSection>
[[Category: Eyzaguirre, J.]]
[[Category: Large Structures]]
[[Category: Ghosh, D.]]
[[Category: Talaromyces purpureogenus]]
[[Category: Jornvall, H.]]
[[Category: Erman M]]
[[Category: Lala, P.]]
[[Category: Eyzaguirre J]]
[[Category: Li, N.]]
[[Category: Ghosh D]]
[[Category: Pangborn, W.]]
[[Category: Jornvall H]]
[[Category: Sawicki, M W.]]
[[Category: Lala P]]
[[Category: Thiel, D J.]]
[[Category: Li N]]
[[Category: Weeks, D R.]]
[[Category: Pangborn W]]
[[Category: Alpha/beta hydrolase]]
[[Category: Sawicki MW]]
[[Category: Esterase]]
[[Category: Thiel DJ]]
[[Category: Serine hydrolase]]
[[Category: Weeks DR]]
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