View source for 28lx


==crystal structure of Dpo31, of a tail-spike protein with depolymerase activity identified in a marine podovirus==
<StructureSection load='28lx' size='340' side='right'caption='[[28lx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[28lx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cobetia_phage_Carin1 Cobetia phage Carin1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=28LX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28LX 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=28lx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28lx OCA], [https://pdbe.org/28lx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28lx RCSB], [https://www.ebi.ac.uk/pdbsum/28lx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28lx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Marine phages are, through the infection of their bacterial hosts, key regulators of microbiome and carbon fluxes in the ocean. Despite their important role, the specific molecular mechanisms that underlie infection are so far understudied. Previously, the podovirus Cobetia marina virus 1 (Carin-1), which infects the marine gamma-proteobacterium C. marina, was shown to display exopolysaccharide depolymerase activity. This activity is likely to mediate degradation of the host capsule to facilitate access to the bacterial membrane receptor, but no corresponding gene could be annotated in the genome of Carin-1 by comparative genomics. Biochemical characterization enabled assignment of this activity to Dpo31, a protein sharing less than 10% sequence identity with any characterized protein. Here, we report the structural domain organization and biochemical characterization of Dpo31, revealing an overall structure that is analogous to podovirus tail-spike proteins, allowing us to locate the depolymerase activity to the D3 domain and to identify original structural features that explain the absence of detectable similarity at the primary-sequence level.

Biochemical and structural characterization of a tail-spike protein with depolymerase activity identified in a marine podovirus.,Sirigu S, Roret T, Mocaer PY, Larocque R, Jouanneau D, Legrand P, Baudoux AC, Czjzek M Acta Crystallogr D Struct Biol. 2026 Jul 1;82(Pt 7):785-799. doi: , 10.1107/S2059798326005425. Epub 2026 Jun 17. PMID:42308020<ref>PMID:42308020</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 28lx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cobetia phage Carin1]]
[[Category: Large Structures]]
[[Category: Baudoux AC]]
[[Category: Czjzek M]]
[[Category: Legrand P]]
[[Category: Roret T]]
[[Category: Sirigu S]]