7a8y
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray crystal structure of Aspartate alpha-decarboxylase in complex with D-Serine== | |
| + | <StructureSection load='7a8y' size='340' side='right'caption='[[7a8y]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7a8y]] 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=7A8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A8Y 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]] 1.75Å</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=7a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a8y OCA], [https://pdbe.org/7a8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a8y RCSB], [https://www.ebi.ac.uk/pdbsum/7a8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a8y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A4Y8GT61_ECOLX A0A4Y8GT61_ECOLX] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.[HAMAP-Rule:MF_00446] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Incoherent neutron spectroscopy, in combination with dynamic light scattering, was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics of Escherichia coli aspartate alpha-decarboxylase (ADC). The X-ray crystal structure of ADC in complex with the D-serine inhibitor was also determined, and molecular dynamics simulations were used to further probe the structural rearrangements that occur as a result of ligand binding. These experiments reveal that D-serine forms hydrogen bonds with some of the active site residues, that higher order oligomers of the ADC tetramer exist on ns-ms time-scales, and also show that ligand binding both affects the ADC internal diffusive dynamics and appears to further increase the size of the higher order oligomers. | ||
| - | + | Structure and diffusive dynamics of aspartate alpha-decarboxylase (ADC) liganded with D-serine in aqueous solution.,Raskar T, Niebling S, Devos JM, Yorke BA, Hartlein M, Huse N, Forsyth VT, Seydel T, Pearson AR Phys Chem Chem Phys. 2022 Aug 31;24(34):20336-20347. doi: 10.1039/d2cp02063g. PMID:35980136<ref>PMID:35980136</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7a8y" style="background-color:#fffaf0;"></div> |
| - | [[Category: Raskar | + | |
| + | ==See Also== | ||
| + | *[[Aspartate decarboxylase 3D structures|Aspartate decarboxylase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Raskar T]] | ||
| + | [[Category: Yorke BA]] | ||
Current revision
X-ray crystal structure of Aspartate alpha-decarboxylase in complex with D-Serine
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