View source for 5f9q


==Crystal structure of the extracellular domain of noncanonic ABC-type transporter YknZ from Gram-positive bacteria==
<StructureSection load='5f9q' size='340' side='right' caption='[[5f9q]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5f9q]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F9Q FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5f9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f9q OCA], [http://pdbe.org/5f9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f9q RCSB], [http://www.ebi.ac.uk/pdbsum/5f9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f9q ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacillus possesses the peptide toxin Sporulation-Delaying Protein (SDP), which can kill cells within a biofilm to support continued growth, thereby delaying the onset of biofilm sporulation. The four-component transporter YknWXYZ acts as a major SDP efflux pump to protect cells against the endogenous SDP toxin, for which YknYZ is a non-canonical ATP-binding cassette (ABC)-type transporter. YknYZ consists of the following two components: (1) an individual protein (YknY) and (2) a respective permease (YknZ). To date, the crystal structure, molecular function, and mechanism of action of the integral membrane protein YknZ remain to be elucidated. In this study, to characterize the structural and biochemical roles of YknZ in the functional assembly of YknWXYZ, we predicted and overexpressed the YknZ extracellular domain. We determined the crystal structure of B. amyloliquefaciens YknZ at a resolution of 2.0 A. The structure revealed that the YknZ extracellular region exhibits significant structural similarity with the MacB periplasmic domain, which is a non-canonical ABC-type transporter in the tripartite macrolide-specific efflux pump in Gram-negative bacteria. We also found that the YknZ extracellular domain can directly bind to an extracellular component of YknX. This structural and biochemical study provides insights into the assembly of YknWXYZ, which may be relevant to understanding cannibalistic peptide toxin resistance in Bacillus and controlling bacterial growth.

The Crystal Structure of the YknZ Extracellular Domain of ABC Transporter YknWXYZ from Bacillus amyloliquefaciens.,Xu Y, Guo J, Wang L, Jiang R, Jin X, Liu J, Fan S, Quan CS, Ha NC PLoS One. 2016 May 31;11(5):e0155846. doi: 10.1371/journal.pone.0155846., eCollection 2016. PMID:27243566<ref>PMID:27243566</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5f9q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fan, S]]
[[Category: Guo, J]]
[[Category: Ha, N C]]
[[Category: Jiang, R]]
[[Category: Jin, X]]
[[Category: Quan, C S]]
[[Category: Xu, Y]]
[[Category: Bacillus amyloliquefacien]]
[[Category: Membrane protein]]
[[Category: Respective permease yknz]]
[[Category: Sdp transporter yknwxyz]]