View source for 6qhw


==Time resolved structural analysis of the full turnover of an enzyme - 4512 ms==
<StructureSection load='6qhw' size='340' side='right'caption='[[6qhw]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qhw]] 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=6QHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QHW 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]] 1.718&#8491;</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>, <scene name='pdbligand=GOA:GLYCOLIC+ACID'>GOA</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=6qhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qhw OCA], [https://pdbe.org/6qhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qhw RCSB], [https://www.ebi.ac.uk/pdbsum/6qhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qhw 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qhw" style="background-color:#fffaf0;"></div>

==See Also==
*[[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]]