1bs9

<table><tr><td colspan='2'>[[1bs9]] is a 1 chain structure with sequence from [https://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]. 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='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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylesterase Acetylesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.6 3.1.1.6] </span></td></tr>

[[https://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>

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bs9" style="background-color:#fffaf0;"></div>

[[Category: Acetylesterase]]

[[Category: Penicillium purpurogenum]]

[[Category: Erman, M]]

[[Category: Eyzaguirre, J]]

[[Category: Ghosh, D]]

[[Category: Jornvall, H]]

[[Category: Lala, P]]

[[Category: Li, N]]

[[Category: Pangborn, W]]

[[Category: Sawicki, M W]]

[[Category: Thiel, D J]]

[[Category: Weeks, D R]]

[[Category: Serine hydrolase]]