1s9u

<table><tr><td colspan='2'>[[1s9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S9U FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>

[[https://www.uniprot.org/uniprot/DMSD_SALTY DMSD_SALTY]] Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein (By similarity).[HAMAP-Rule:MF_00940]

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== Publication Abstract from PubMed ==

The DmsD protein is necessary for the biogenesis of dimethyl sulphoxide (DMSO) reductase in many prokaryotes. It performs a critical chaperone function initiated through its binding to the twin-arginine signal peptide of DmsA, the catalytic subunit of DMSO reductase. Upon binding to DmsD, DmsA is translocated to the periplasm via the so-called twin-arginine translocation (Tat) pathway. Here we report the 1.38 A crystal structure of the protein DmsD from Salmonella typhimurium and compare it with a close functional homolog, TorD. DmsD has an all-alpha fold structure with a notable helical extension located at its N-terminus with two solvent exposed hydrophobic residues. A major difference between DmsD and TorD is that TorD structure is a domain-swapped dimer, while DmsD exists as a monomer. Nevertheless, these two proteins have a number of common features suggesting they function by using similar mechanisms. A possible signal peptide-binding site is proposed based on structural similarities. Computational analysis was used to identify a potential GTP binding pocket on similar surfaces of DmsD and TorD structures.

The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway.,Qiu Y, Zhang R, Binkowski TA, Tereshko V, Joachimiak A, Kossiakoff A Proteins. 2008 May 1;71(2):525-33. PMID:18175314<ref>PMID:18175314</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Salty]]

[[Category: Collart, F]]

[[Category: Joachimiak, A]]

[[Category: Kim, Y]]

[[Category: Kossiakoff, A]]

[[Category: Structural genomic]]

[[Category: Qiu, Y]]

[[Category: Tereshko, V]]

[[Category: Zhang, R]]

[[Category: Unknown function]]