1bs9: Difference between revisions

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<StructureSection load='1bs9' size='340' side='right'caption='[[1bs9]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
<StructureSection load='1bs9' size='340' side='right'caption='[[1bs9]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 1.1&#8491;</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>
<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>
<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>
</table>
== Function ==
== Function ==
[[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>
[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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</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].
</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="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.
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>
</div>
<div class="pdbe-citations 1bs9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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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: Jornvall, H]]
[[Category: Jornvall H]]
[[Category: Lala, P]]
[[Category: Lala P]]
[[Category: Li, N]]
[[Category: Li N]]
[[Category: Pangborn, W]]
[[Category: Pangborn W]]
[[Category: Sawicki, M W]]
[[Category: Sawicki MW]]
[[Category: Thiel, D J]]
[[Category: Thiel DJ]]
[[Category: Weeks, D R]]
[[Category: Weeks DR]]
[[Category: Alpha/beta hydrolase]]
[[Category: Esterase]]
[[Category: Serine hydrolase]]

Revision as of 18:35, 13 March 2024

ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMSACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS

Structural highlights

1bs9 is a 1 chain structure with sequence from Talaromyces purpureogenus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ 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

1bs9, resolution 1.10Å

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