8q4y

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'''Unreleased structure'''
 
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The entry 8q4y is ON HOLD
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==Beta-galactosidase from Bacillus circulans conformational state 1==
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<StructureSection load='8q4y' size='340' side='right'caption='[[8q4y]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8q4y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q4Y FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8q4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q4y OCA], [https://pdbe.org/8q4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q4y RCSB], [https://www.ebi.ac.uk/pdbsum/8q4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q4y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/E5RWQ2_NIACI E5RWQ2_NIACI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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beta-Galactosidase from Bacillus circulans ATCC 31382 (BgaD) is a biotechnologically important enzyme for the synthesis of beta-galactooligosaccharides (GOS). Among its four isoforms, isoform A (BgaD-A) has distinct synthetic properties. Here, we present cryoelectron microscopy (cryo-EM) structures of BgaD-A and compare them with the known X-ray crystal structure of isoform D (BgaD-D), revealing substantial structural divergences between the two isoforms. In contrast to BgaD-D, BgaD-A features a flexible Big-4 domain and another enigmatic domain. The newly identified flexible region in BgaD-A is termed as "barrier domain 8," and serves as a barricade, obstructing the access of longer oligosaccharide substrates into the active site of BgaD-A. The transgalactosylation reactions catalyzed by both isoforms revealed that BgaD-A has a higher selectivity than BgaD-D in the earlier stages of the reaction and is prevailingly directed to shorter galactooligosaccharides. This study improves our understanding of the structural determinants governing beta-galactosidase catalysis, with implications for tailored GOS production.
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Authors:
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The variable structural flexibility of the Bacillus circulans beta-galactosidase isoforms determines their unique functionalities.,Hovorkova M, Kascakova B, Petraskova L, Havlickova P, Novacek J, Pinkas D, Gardian Z, Kren V, Bojarova P, Smatanova IK Structure. 2024 Sep 26:S0969-2126(24)00374-5. doi: 10.1016/j.str.2024.09.005. PMID:39353423<ref>PMID:39353423</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8q4y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Niallia circulans]]
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[[Category: Bojarova P]]
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[[Category: Gardian Z]]
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[[Category: Hovorkova M]]
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[[Category: Kascakova B]]
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[[Category: Kren V]]
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[[Category: Kuta Smatanova I]]
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[[Category: Novacek J]]
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[[Category: Petraskova L]]
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[[Category: Pinkas D]]

Current revision

Beta-galactosidase from Bacillus circulans conformational state 1

PDB ID 8q4y

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