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==Crystal structure of a monomeric beta-xylosidase from Caulobacter crescentus CB15==
==Crystal structure of a monomeric beta-xylosidase from Caulobacter crescentus CB15==
<StructureSection load='4ekj' size='340' side='right' caption='[[4ekj]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4ekj' size='340' side='right'caption='[[4ekj]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ekj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EKJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ekj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EKJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.5&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Itgav, CC_2357 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides])</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'>[http://en.wikipedia.org/wiki/Xylan_1,4-beta-xylosidase Xylan 1,4-beta-xylosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.37 3.2.1.37] </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=4ekj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekj OCA], [https://pdbe.org/4ekj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ekj RCSB], [https://www.ebi.ac.uk/pdbsum/4ekj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ekj ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ekj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ekj RCSB], [http://www.ebi.ac.uk/pdbsum/4ekj PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q9A5U0_CAUVC Q9A5U0_CAUVC]
beta-Xylosidases (EC 3.2.1.37) are among the principal glycosyl hydrolases involved in the breakdown of hemicelluloses, catalyzing the reduction of xylooligosaccharides to free xylose. All GH39 beta-xylosidases structurally characterized to date display a modular multi-domain organization that assembles a tetrameric quaternary structure. In this work, the crystal structure and the SAXS molecular envelope of a new GH39 beta-xylosidase from Caulobacter crescentus (CcXynB2) have been determined. Interestingly, CcXynB2 is a monomer in solution and comparative structural analyses suggest that the shortened C-terminus prevents the formation of a stable tetramer. Moreover, CcXynB2 has a longer loop from the auxiliary domain (the long alpha-helix-containing loop) which makes a number of polar and hydrophobic contacts with the parental (alpha/beta)(8)-barrel domain, modifying the accessibility and the molecular topography of the catalytic interface. These interactions also maintain the accessory domain tightly linked to the catalytic core, which may be important for enzyme function and stability.
 
The accessory domain changes the accessibility and molecular topography of the catalytic interface in monomeric GH39 beta-xylosidases.,Santos CR, Polo CC, Correa JM, Simao Rde C, Seixas FA, Murakami MT Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1339-45. Epub 2012 Sep, 18. PMID:22993088<ref>PMID:22993088</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Xylosidase|Xylosidase]]
*[[Xylosidase 3D structures|Xylosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caulobacter vibrioides]]
[[Category: Caulobacter vibrioides]]
[[Category: Xylan 1,4-beta-xylosidase]]
[[Category: Large Structures]]
[[Category: Correa, J M]]
[[Category: Correa JM]]
[[Category: Murakami, M T]]
[[Category: Murakami MT]]
[[Category: Polo, C C]]
[[Category: Polo CC]]
[[Category: Santos, C R]]
[[Category: Santos CR]]
[[Category: Seixas, F A.V]]
[[Category: Seixas FAV]]
[[Category: Simao, R C.G]]
[[Category: Simao RCG]]
[[Category: Hemicellulase]]
[[Category: Hydrolase]]
[[Category: Tim-barrel fold]]

Latest revision as of 15:03, 14 March 2024

Crystal structure of a monomeric beta-xylosidase from Caulobacter crescentus CB15

4ekj, resolution 2.50Å

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