View source for 3oba


==Structure of the beta-galactosidase from Kluyveromyces lactis==
<StructureSection load='3oba' size='340' side='right'caption='[[3oba]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3oba]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OBA 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]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN3:MANGANESE+(III)+ION'>MN3</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=3oba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oba OCA], [https://pdbe.org/3oba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oba RCSB], [https://www.ebi.ac.uk/pdbsum/3oba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oba ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BGAL_KLULA BGAL_KLULA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Galactosidase or lactase is a very important enzyme in the food industry, being that from the yeast Kluyveromyces lactis the most widely used. Here we report its three-dimensional structure both in the free state and complexed with the product galactose. The monomer folds into five domains in a pattern conserved with the prokaryote enzymes of the GH2 family, although two long insertions in domains 2 and 3 are unique and related to oligomerization and specificity. The tetrameric enzyme is a dimer of dimers, with higher dissociation energy for the dimers than for its assembly. Two active centers are located at the interface within each dimer in a narrow channel. The insertion at domain 3 protrudes into this channel and makes putative links with the aglycone moiety of docked lactose. In spite of common structural features related to function, the determinants of the reaction mechanism proposed for Escherichia coli beta-galactosidase are not found in the active site of the K. lactis enzyme. This is the first X-ray crystal structure for a beta-galactosidase used in food processing.

Structural basis of specificity in tetrameric Kluyveromyces lactis beta-galactosidase.,Pereira-Rodriguez A, Fernandez-Leiro R, Gonzalez-Siso MI, Cerdan ME, Becerra M, Sanz-Aparicio J J Struct Biol. 2011 Dec 13. PMID:22193516<ref>PMID:22193516</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oba" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kluyveromyces lactis]]
[[Category: Large Structures]]
[[Category: Becerra M]]
[[Category: Cerdan ME]]
[[Category: Fernandez-Leiro R]]
[[Category: Gonzalez-Siso I]]
[[Category: Pereira-Rodriguez A]]
[[Category: Sanz-Aparicio J]]