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4ckd

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'''Unreleased structure'''
 
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The entry 4ckd is ON HOLD until sometime in the future
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==Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.==
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<SX load='4ckd' size='340' side='right' viewer='molstar' caption='[[4ckd]], [[Resolution|resolution]] 13.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ckd]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CKD FirstGlance]. <br>
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</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=4ckd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ckd OCA], [https://pdbe.org/4ckd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ckd RCSB], [https://www.ebi.ac.uk/pdbsum/4ckd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ckd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/BGAL_ECOLI BGAL_ECOLI]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Binding of a single-chain Fv antibody to Escherichia coli beta-galactosidase (beta-gal) is known to stabilize the enzyme and activate several inactive point mutants, historically called antibody-mediated enzyme formation mutants. To understand the nature of this activation, we have determined by electron cryo-microscopy the structure of the complex between beta-gal and the antibody scFv13R4. Our structure localizes the scFv13R4 binding site to the crevice between domains 1 and 3 in each beta-gal subunit. The mutations that scFv13R4 counteracts are located between the antibody binding site and the active site of beta-gal, at one end of the TIM-barrel that forms domain 3 where the substrate lactose is hydrolyzed. The mode of binding suggests how scFv stabilizes both the active site of beta-gal and the tetrameric state.
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Authors: Vinothkumar, K.R., McMullan, G., Henderson, R.
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Molecular Mechanism of Antibody-Mediated Activation of beta-galactosidase.,Vinothkumar KR, McMullan G, Henderson R Structure. 2014 Mar 4. pii: S0969-2126(14)00039-2. doi:, 10.1016/j.str.2014.01.011. PMID:24613486<ref>PMID:24613486</ref>
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Description: Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ckd" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Antibody 3D structures|Antibody 3D structures]]
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*[[Galactosidase 3D structures|Galactosidase 3D structures]]
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*[[3D structures of non-human antibody|3D structures of non-human antibody]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Henderson R]]
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[[Category: McMullan G]]
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[[Category: Vinothkumar KR]]

Current revision

Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.

4ckd, resolution 13.00Å

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