3tts: Difference between revisions
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==Crystal structure of beta-galactosidase from Bacillus circulans sp. alkalophilus== | ==Crystal structure of beta-galactosidase from Bacillus circulans sp. alkalophilus== | ||
<StructureSection load='3tts' size='340' side='right' caption='[[3tts]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3tts' size='340' side='right' caption='[[3tts]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tty|3tty]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tty|3tty]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3tts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tts OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tts RCSB], [http://www.ebi.ac.uk/pdbsum/3tts PDBsum]</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=3tts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tts OCA], [http://pdbe.org/3tts PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tts RCSB], [http://www.ebi.ac.uk/pdbsum/3tts PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tts ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3tts" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 23:50, 11 August 2016
Crystal structure of beta-galactosidase from Bacillus circulans sp. alkalophilusCrystal structure of beta-galactosidase from Bacillus circulans sp. alkalophilus
Structural highlights
Publication Abstract from PubMedCrystal structures of native and alpha-D-galactose -bound Bacillus circulans sp. alkalophilusbeta-galactosidase (Bca-beta-gal) were determined at 2.40 A and 2.25 A resolutions, respectively. Bca-beta-gal is a member of family 42 of glycoside hydrolases and it forms a 460 kDa hexameric structure in crystal. The protein consists of three domains in which the catalytic domain has an (alpha/beta)(8) -barrel structure with a cluster of sulfur-rich residues inside the beta-barrel. The shape of the active site is clearly more open compared to the only homological structure available in the Protein Data Bank. This is due to the number of large differences in the loops that connect the C-terminal ends of the beta-strands to N-terminal ends of the alpha-helices within the (alpha/beta)(8) -barrel. The complex structure shows that galactose has bound to the active site as an alpha-anomer and induced clear conformational changes in the active site. The implications of alpha-D-galactose binding to the catalytic mechanism is discussed. In addition, we suggest that beta-galactosidases only utilize mainly reverse hydrolysis mechanism for the synthesis of galacto-oligosaccharides. Structural analysis, enzymatic characterization, and catalytic mechanisms of beta-galactosidase from Bacillus circulans sp. alkalophilus.,Maksimainen M, Paavilainen S, Hakulinen N, Rouvinen J FEBS J. 2012 Mar 3. doi: 10.1111/j.1742-4658.2012.08555.x. PMID:22385475[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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