6e8a: Difference between revisions

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'''Unreleased structure'''


The entry 6e8a is ON HOLD  until Paper Publication
==Crystal structure of DcrB from Salmonella enterica at 1.92 Angstroms resolution==
<StructureSection load='6e8a' size='340' side='right' caption='[[6e8a]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6e8a]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E8A FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8a OCA], [http://pdbe.org/6e8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e8a RCSB], [http://www.ebi.ac.uk/pdbsum/6e8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8a ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DcrB is an 18kDa lipoprotein that contains a single domain of unknown function. DcrB is found within Enterobacteriaceae, a family of Gram-negative bacteria which includes pathogens that can cause food-borne illness and hospital-acquired infections. In Salmonella enterica serovar Typhimurium, DcrB is up-regulated by conditions that promote the production of known virulence factors. We determined the structure of a truncated form of DcrB from Salmonella to 1.92A resolution by X-ray crystallography. This truncated form, DcrBDelta37, contains the entire domain of unknown function but lacks the lipoprotein signal sequence (residues 1-20) as well as residues 21-37. The DcrBDelta37 monomer contains the Mog1p/PsbP-like fold, which is found in functionally diverse proteins in mammals, yeast, plants, and cyanobacteria. Interestingly, DcrBDelta37 crystallized as a domain-swapped homodimer in which the N-terminal beta-hairpin extends from one protomer to interact with the core of the second protomer. This domain-swapping indicates that the N-terminal portion of the Mog1p/PsbP-like fold likely has conformational flexibility. Overall, our results provide the first example of an enterobacterial protein that contains the Mog1p/PsbP-like fold and expands knowledge of the structural and phylogenetic diversity of Mog1p/PsbP-like proteins.


Authors:  
The structure of DcrB, a lipoprotein from Salmonella enterica, reveals flexibility in the N-terminal segment of the Mog1p/PsbP-like fold.,Rasmussen DM, Soens RW, Davie TJ, Vaneerd CK, Bhattacharyya B, May JF J Struct Biol. 2018 Oct 16. pii: S1047-8477(18)30278-8. doi:, 10.1016/j.jsb.2018.10.005. PMID:30339832<ref>PMID:30339832</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6e8a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bhattacharyya, B]]
[[Category: May, J F]]
[[Category: Rasmussen, D M]]
[[Category: Soens, R W]]
[[Category: Mog1/psbp-like fold lipoprotein]]
[[Category: Unknown function]]
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