3s2c: Difference between revisions

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<StructureSection load='3s2c' size='340' side='right'caption='[[3s2c]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3s2c' size='340' side='right'caption='[[3s2c]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3s2c]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thep1 Thep1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S2C FirstGlance]. <br>
<table><tr><td colspan='2'>[[3s2c]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S2C FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tpet_0631 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=390874 THEP1])</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]] 3&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </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=3s2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s2c OCA], [https://pdbe.org/3s2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s2c RCSB], [https://www.ebi.ac.uk/pdbsum/3s2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s2c 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=3s2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s2c OCA], [https://pdbe.org/3s2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s2c RCSB], [https://www.ebi.ac.uk/pdbsum/3s2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s2c ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A5IKC8_THEP1 A5IKC8_THEP1]
alpha-L-arabinofuranosidases (EC 3.2.1.55) participate in the degradation of a variety of L-arabinose-containing polysaccharides and interact synergistically with other hemicellulases in the production of oligosaccharides and bioconversion of lignocellulosic biomass into biofuels. In this work, the structure of a novel thermostable family 51 (GH51) alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 (TpAraF) was determined at 3.1 A resolution. The TpAraF tertiary structure consists of an (alpha/beta)-barrel catalytic core associated with a C-terminal beta-sandwich domain, which is stabilized by hydrophobic contacts. In contrast to other structurally characterized GH51 AraFs, the accessory domain of TpAraF is intimately linked to the active site by a long beta-hairpin motif, which modifies the catalytic cavity in shape and volume. Sequence and structural analyses indicate that this motif is unique to Thermotoga AraFs. Small angle X-ray scattering investigation showed that TpAraF assembles as a hexamer in solution and is preserved at the optimum catalytic temperature, 65 degrees C, suggesting functional significance. Crystal packing analysis shows that the biological hexamer encompasses a dimer of trimers and the multiple oligomeric interfaces are predominantly fashioned by polar and electrostatic contacts.
 
Structure of a novel thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1.,Souza TA, Santos CR, Souza AR, Oldiges DP, Ruller R, Prade RA, Squina FM, Murakami MT Protein Sci. 2011 Sep;20(9):1632-7. doi: 10.1002/pro.693. Epub 2011 Aug 3. PMID:21796714<ref>PMID:21796714</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3s2c" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Non-reducing end alpha-L-arabinofuranosidase]]
[[Category: Thermotoga petrophila RKU-1]]
[[Category: Thep1]]
[[Category: Murakami MT]]
[[Category: Murakami, M T]]
[[Category: Oldiges DP]]
[[Category: Oldiges, D P]]
[[Category: Prade RA]]
[[Category: Prade, R A]]
[[Category: Ruller R]]
[[Category: Ruller, R]]
[[Category: Santos CR]]
[[Category: Santos, C R]]
[[Category: Souza AR]]
[[Category: Souza, A R]]
[[Category: Souza TACB]]
[[Category: Souza, T A.C B]]
[[Category: Squina FM]]
[[Category: Squina, F M]]
[[Category: Alpha-l-arabinofuranosidase]]
[[Category: Glycosyl hydrolase 51 family]]
[[Category: Hydrolase]]
[[Category: Tim-barrel and jelly-roll domain]]

Latest revision as of 12:43, 14 March 2024

Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1

3s2c, resolution 3.00Å

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