6b58: Difference between revisions
New page: '''Unreleased structure''' The entry 6b58 is ON HOLD Authors: Sharma, P., Iverson, T.M. Description: FrdA-SdhE assembly intermediate Category: Unreleased Structures [[Category: Sha... |
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==FrdA-SdhE assembly intermediate== | |||
<StructureSection load='6b58' size='340' side='right'caption='[[6b58]], [[Resolution|resolution]] 2.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6b58]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B58 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]] 2.611Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=PBF:PARA-(BENZOYL)-PHENYLALANINE'>PBF</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6b58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b58 OCA], [https://pdbe.org/6b58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b58 RCSB], [https://www.ebi.ac.uk/pdbsum/6b58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b58 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Flavin is covalently attached to the protein scaffold in ~10% of flavoenzymes. However, the mechanism of covalent modification is unclear, due in part to challenges in stabilizing assembly intermediates. Here, we capture the structure of an assembly intermediate of the Escherichia coli Complex II (quinol:fumarate reductase (FrdABCD)). The structure contains the E. coli FrdA subunit bound to covalent FAD and crosslinked with its assembly factor, SdhE. The structure contains two global conformational changes as compared to prior structures of the mature protein: the rotation of a domain within the FrdA subunit, and the destabilization of two large loops of the FrdA subunit, which may create a tunnel to the active site. We infer a mechanism for covalent flavinylation. As supported by spectroscopic and kinetic analyses, we suggest that SdhE shifts the conformational equilibrium of the FrdA active site to disfavor succinate/fumarate interconversion and enhance covalent flavinylation. | |||
Crystal structure of an assembly intermediate of respiratory Complex II.,Sharma P, Maklashina E, Cecchini G, Iverson TM Nat Commun. 2018 Jan 18;9(1):274. doi: 10.1038/s41467-017-02713-8. PMID:29348404<ref>PMID:29348404</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6b58" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Iverson TM]] | |||
[[Category: Sharma P]] | |||
Latest revision as of 17:33, 4 October 2023
FrdA-SdhE assembly intermediateFrdA-SdhE assembly intermediate
Structural highlights
FunctionFRDA_ECOLI Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Publication Abstract from PubMedFlavin is covalently attached to the protein scaffold in ~10% of flavoenzymes. However, the mechanism of covalent modification is unclear, due in part to challenges in stabilizing assembly intermediates. Here, we capture the structure of an assembly intermediate of the Escherichia coli Complex II (quinol:fumarate reductase (FrdABCD)). The structure contains the E. coli FrdA subunit bound to covalent FAD and crosslinked with its assembly factor, SdhE. The structure contains two global conformational changes as compared to prior structures of the mature protein: the rotation of a domain within the FrdA subunit, and the destabilization of two large loops of the FrdA subunit, which may create a tunnel to the active site. We infer a mechanism for covalent flavinylation. As supported by spectroscopic and kinetic analyses, we suggest that SdhE shifts the conformational equilibrium of the FrdA active site to disfavor succinate/fumarate interconversion and enhance covalent flavinylation. Crystal structure of an assembly intermediate of respiratory Complex II.,Sharma P, Maklashina E, Cecchini G, Iverson TM Nat Commun. 2018 Jan 18;9(1):274. doi: 10.1038/s41467-017-02713-8. PMID:29348404[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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