6vvr: Difference between revisions
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<StructureSection load='6vvr' size='340' side='right'caption='[[6vvr]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6vvr' size='340' side='right'caption='[[6vvr]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6vvr]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6vvr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_trematum Bordetella trematum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VVR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vvr OCA], [https://pdbe.org/6vvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vvr RCSB], [https://www.ebi.ac.uk/pdbsum/6vvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vvr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A157L8Q0_9BORD A0A157L8Q0_9BORD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Bordetella trematum]] | [[Category: Bordetella trematum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Medellin | [[Category: Medellin BP]] | ||
[[Category: Whitman | [[Category: Whitman CP]] | ||
[[Category: Zhang | [[Category: Zhang YJ]] | ||
Latest revision as of 11:21, 11 October 2023
Q0 fused 4-OT wild type symmetric trimerQ0 fused 4-OT wild type symmetric trimer
Structural highlights
FunctionPublication Abstract from PubMedTautomerase superfamily (TSF) members are constructed from a single beta-alpha-beta unit or two consecutively joined beta-alpha-beta units. This pattern prevails throughout the superfamily consisting of more than 11000 members where homo- or heterohexamers are localized in the 4-oxalocrotonate tautomerase (4-OT) subgroup and trimers are found in the other four subgroups. One exception is a subset of sequences that are double the length of the short 4-OTs in the 4-OT subgroup, where the coded proteins form trimers. Characterization of two members revealed an interesting dichotomy. One is a symmetric trimer, whereas the other is an asymmetric trimer. One monomer is flipped 180 degrees relative to the other two monomers so that three unique protein-protein interfaces are created that are composed of different residues. A bioinformatics analysis of the fused 4-OT subset shows a further division into two clusters with a total of 133 sequences. The analysis showed that members of one cluster (86 sequences) have more salt bridges if the asymmetric trimer forms, whereas the members of the other cluster (47 sequences) have more salt bridges if the symmetric trimer forms. This hypothesis was examined by the kinetic and structural characterization of two proteins within each cluster. As predicted, all four proteins function as 4-OTs, where two assemble into asymmetric trimers (designated R7 and F6) and two form symmetric trimers (designated W0 and Q0). These findings can be extended to the other sequences in the two clusters in the fused 4-OT subset, thereby annotating their oligomer properties and activities. Structural Basis for the Asymmetry of a 4-Oxalocrotonate Tautomerase Trimer.,Medellin BP, Lancaster EB, Brown SD, Rakhade S, Babbitt PC, Whitman CP, Zhang YJ Biochemistry. 2020 Apr 13. doi: 10.1021/acs.biochem.0c00211. PMID:32242662[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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