View source for 8ooh


==Cryo-EM map of the focused refinement of the subfamily III haloalkane dehalogenase from Haloferax mediterranei dimer forming hexameric assembly.==
<StructureSection load='8ooh' size='340' side='right'caption='[[8ooh]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ooh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_mediterranei Haloferax mediterranei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OOH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7&#8491;</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=8ooh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ooh OCA], [https://pdbe.org/8ooh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ooh RCSB], [https://www.ebi.ac.uk/pdbsum/8ooh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ooh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I3R766_HALMT I3R766_HALMT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Haloalkane dehalogenase (HLD) enzymes employ an S(N) 2 nucleophilic substitution mechanism to erase halogen substituents in diverse organohalogen compounds. Subfamily I and II HLDs are well-characterized enzymes, but a mode and purpose of multimerization of subfamily III HLDs are unknown. Here we probe the structural organization of DhmeA, a subfamily III HLD-like enzyme from the archaeon Haloferax mediterranei, by combining cryo-electron microscopy (cryo-EM) and X-ray crystallography. We show that full-length wild-type DhmeA forms diverse quaternary structures, ranging from small oligomers to large supramolecular ring-like assemblies of various sizes and symmetries. We optimized sample preparation steps, enabling three-dimensional reconstructions of an oligomeric species by single-particle cryo-EM. Moreover, we engineered a crystallizable mutant (DhmeA(DeltaGG) ) that provided diffraction-quality crystals. The 3.3 A crystal structure reveals that DhmeA(DeltaGG) forms a ring-like 20-mer structure with outer and inner diameter of ~200 A and ~80 A, respectively. An enzyme homodimer represents a basic repeating building unit of the crystallographic ring. Three assembly interfaces (dimerization, tetramerization and multimerization) were identified to form the supramolecular ring that displays a negatively charged exterior, while its interior part harboring catalytic sites is positively charged. Localization and exposure of catalytic machineries suggest a possible processing of large negatively charged macromolecular substrates. This article is protected by copyright. All rights reserved.

Multimeric structure of a subfamily III haloalkane dehalogenase-like enzyme solved by combination of cryo-EM and X-ray crystallography.,Chmelova K, Gao T, Polak M, Schenkmayerova A, Croll TI, Shaikh TR, Skarupova J, Chaloupkova R, Diederichs K, Read RJ, Damborsky J, Novacek J, Marek M Protein Sci. 2023 Aug 13:e4751. doi: 10.1002/pro.4751. PMID:37574754<ref>PMID:37574754</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ooh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Haloferax mediterranei]]
[[Category: Large Structures]]
[[Category: Chmelova K]]
[[Category: Marek M]]
[[Category: Novacek J]]
[[Category: Polak M]]