6qhq: Difference between revisions
New page: '''Unreleased structure''' The entry 6qhq is ON HOLD Authors: Schulz, E.C., Mehrabi, P., Pai, E.F., Miller, D. Description: Time resolved structural analysis of the full turnover of an... |
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==Time resolved structural analysis of the full turnover of an enzyme - 1128 ms== | |||
<StructureSection load='6qhq' size='340' side='right'caption='[[6qhq]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qhq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QHQ 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]] 1.735Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAH:FLUOROACETIC+ACID'>FAH</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=6qhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qhq OCA], [https://pdbe.org/6qhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qhq RCSB], [https://www.ebi.ac.uk/pdbsum/6qhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qhq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DEHA_RHOPA DEHA_RHOPA] Catalyzes the hydrolytic defluorination of fluoroacetate to produce glycolate. Has lower activity towards bromoacetate and chloroacetate.<ref>PMID:21510690</ref> <ref>PMID:21510690</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A comprehensive understanding of protein function demands correlating structure and dynamic changes. Using time-resolved serial synchrotron crystallography, we visualized half-of-the-sites reactivity and correlated molecular-breathing motions in the enzyme fluoroacetate dehalogenase. Eighteen time points from 30 milliseconds to 30 seconds cover four turnover cycles of the irreversible reaction. They reveal sequential substrate binding, covalent-intermediate formation, setup of a hydrolytic water molecule, and product release. Small structural changes of the protein mold and variations in the number and placement of water molecules accompany the various chemical steps of catalysis. Triggered by enzyme-ligand interactions, these repetitive changes in the protein framework's dynamics and entropy constitute crucial components of the catalytic machinery. | |||
Time-resolved crystallography reveals allosteric communication aligned with molecular breathing.,Mehrabi P, Schulz EC, Dsouza R, Muller-Werkmeister HM, Tellkamp F, Miller RJD, Pai EF Science. 2019 Sep 13;365(6458):1167-1170. doi: 10.1126/science.aaw9904. PMID:31515393<ref>PMID:31515393</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6qhq" style="background-color:#fffaf0;"></div> | ||
[[Category: Mehrabi | |||
[[Category: Miller | ==See Also== | ||
[[Category: Schulz | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhodopseudomonas palustris]] | |||
[[Category: Mehrabi P]] | |||
[[Category: Miller D]] | |||
[[Category: Pai EF]] | |||
[[Category: Schulz EC]] | |||
Latest revision as of 15:01, 24 January 2024
Time resolved structural analysis of the full turnover of an enzyme - 1128 msTime resolved structural analysis of the full turnover of an enzyme - 1128 ms
Structural highlights
FunctionDEHA_RHOPA Catalyzes the hydrolytic defluorination of fluoroacetate to produce glycolate. Has lower activity towards bromoacetate and chloroacetate.[1] [2] Publication Abstract from PubMedA comprehensive understanding of protein function demands correlating structure and dynamic changes. Using time-resolved serial synchrotron crystallography, we visualized half-of-the-sites reactivity and correlated molecular-breathing motions in the enzyme fluoroacetate dehalogenase. Eighteen time points from 30 milliseconds to 30 seconds cover four turnover cycles of the irreversible reaction. They reveal sequential substrate binding, covalent-intermediate formation, setup of a hydrolytic water molecule, and product release. Small structural changes of the protein mold and variations in the number and placement of water molecules accompany the various chemical steps of catalysis. Triggered by enzyme-ligand interactions, these repetitive changes in the protein framework's dynamics and entropy constitute crucial components of the catalytic machinery. Time-resolved crystallography reveals allosteric communication aligned with molecular breathing.,Mehrabi P, Schulz EC, Dsouza R, Muller-Werkmeister HM, Tellkamp F, Miller RJD, Pai EF Science. 2019 Sep 13;365(6458):1167-1170. doi: 10.1126/science.aaw9904. PMID:31515393[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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