7o87: Difference between revisions
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==Crystal structure of holo-F210W mutant of Hydroxy ketone aldolase (SwHKA) from Sphingomonas wittichii RW1 in complex with hydroxypyruvate== | |||
<StructureSection load='7o87' size='340' side='right'caption='[[7o87]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7o87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizorhabdus_wittichii_RW1 Rhizorhabdus wittichii RW1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O87 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7o87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o87 OCA], [https://pdbe.org/7o87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o87 RCSB], [https://www.ebi.ac.uk/pdbsum/7o87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o87 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Regulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally required to tune the metal cofactor's properties by allosteric regulation. Here structural analysis of hydroxyketoacid aldolase from Sphingomonas wittichii RW1 ( Sw HKA) revealed a dynamic movement of the metal cofactor between two coordination spheres without protein scaffold rearrangements. In its resting state configuration (M 2+ R ), the metal constitutes an integral part of the dimer interface within the overall hexameric assembly, but sterical constraints do not allow for substrate binding. Conversely, a second coordination sphere constitutes the catalytically active state (M 2+ A ) at 2.4 A distance. Bidentate coordination of a ketoacid substrate to M 2+ A affords the overall lowest energy complex, which drives the transition from M 2+ R to M 2+ A . While not described earlier, this type of regulation may be widespread and largely overlooked due to low occupancy of some of its states in protein crystal structures. | |||
Substrate Induced Movement of the Metal Cofactor between Active and Resting State.,Marsden SR, Wijma HJ, Mohr MKF, Justo I, Hagedoorn PL, Laustsen J, Jeffries CM, Svergun D, Mestrom L, McMillan DGG, Bento I, Hanefeld U Angew Chem Int Ed Engl. 2022 Oct 10. doi: 10.1002/anie.202213338. PMID:36214476<ref>PMID:36214476</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7o87" style="background-color:#fffaf0;"></div> | ||
[[Category: Bento | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Rhizorhabdus wittichii RW1]] | |||
[[Category: Bento I]] | |||
[[Category: Hanefeld U]] | |||
[[Category: Justo I]] | |||
[[Category: Laustsen J]] | |||
[[Category: Marsden SR]] | |||
Latest revision as of 15:46, 1 February 2024
Crystal structure of holo-F210W mutant of Hydroxy ketone aldolase (SwHKA) from Sphingomonas wittichii RW1 in complex with hydroxypyruvateCrystal structure of holo-F210W mutant of Hydroxy ketone aldolase (SwHKA) from Sphingomonas wittichii RW1 in complex with hydroxypyruvate
Structural highlights
Publication Abstract from PubMedRegulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally required to tune the metal cofactor's properties by allosteric regulation. Here structural analysis of hydroxyketoacid aldolase from Sphingomonas wittichii RW1 ( Sw HKA) revealed a dynamic movement of the metal cofactor between two coordination spheres without protein scaffold rearrangements. In its resting state configuration (M 2+ R ), the metal constitutes an integral part of the dimer interface within the overall hexameric assembly, but sterical constraints do not allow for substrate binding. Conversely, a second coordination sphere constitutes the catalytically active state (M 2+ A ) at 2.4 A distance. Bidentate coordination of a ketoacid substrate to M 2+ A affords the overall lowest energy complex, which drives the transition from M 2+ R to M 2+ A . While not described earlier, this type of regulation may be widespread and largely overlooked due to low occupancy of some of its states in protein crystal structures. Substrate Induced Movement of the Metal Cofactor between Active and Resting State.,Marsden SR, Wijma HJ, Mohr MKF, Justo I, Hagedoorn PL, Laustsen J, Jeffries CM, Svergun D, Mestrom L, McMillan DGG, Bento I, Hanefeld U Angew Chem Int Ed Engl. 2022 Oct 10. doi: 10.1002/anie.202213338. PMID:36214476[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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