View source for 4ml1


==Disulfide isomerase (DsbP) from multidrug resistance IncA/C transferable plasmid in oxidized state (P212121 space group)==
<StructureSection load='4ml1' size='340' side='right'caption='[[4ml1]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ml1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ML1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ML1 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]] 1.978&#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=4ml1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ml1 OCA], [https://pdbe.org/4ml1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ml1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ml1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ml1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A6GV51_KLEPN A6GV51_KLEPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The multidrug resistance-encoding IncA/C conjugative plasmids disseminate antibiotic resistance genes among clinically relevant enteric bacteria. A plasmid-encoded disulfide isomerase is associated with conjugation. Sequence analysis of several IncA/C plasmids and IncA/C related integrative and conjugative elements (ICE) from commensal and pathogenic bacteria identified a conserved DsbC/DsbG homolog (DsbP). The crystal structure of DsbP reveals an N-terminal domain, a linker region and a C-terminal catalytic domain. A DsbP homodimer is formed through domain-swapping of two DsbP N-terminal domains. The catalytic domain incorporates a thioredoxin fold with characteristic CXXC and cisPro motifs. Overall, the structure and redox properties of DsbP diverge from the Escherichia coli DsbC and DsbG disulfide isomerases. Specifically, the V-shaped dimer of DsbP is inverted compared to EcDsbC and EcDsbG. In addition, the redox potential of DsbP (-161 mV) is more reducing than EcDsbC (-130 mV) and EcDsbG (-126 mV). Other catalytic properties of DsbP more closely resemble those of EcDsbG than EcDsbC. These catalytic differences are in part a consequence of the unusual active site motif of DsbP (CAVC); substitution to the EcDsbC-like (CGYC) motif converts the catalytic properties to those of EcDsbC. Structural comparison of the 12 independent subunit structures of DsbP that we determined revealed that conformational changes in the linker region contribute to mobility of the catalytic domain, providing mechanistic insight into DsbP function. In summary, our data reveal that the conserved plasmid-encoded DsbP protein is a bona fide disulfide isomerase and suggest that a dedicated oxidative folding enzyme is important for conjugative plasmid transfer.

The multidrug resistance IncA/C transferable plasmid encodes a novel domain swapped dimeric protein disulfide isomerase.,Premkumar L, Kurth F, Neyer S, Schembri MA, Martin JL J Biol Chem. 2013 Dec 5. PMID:24311786<ref>PMID:24311786</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ml1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Kurth F]]
[[Category: Martin JL]]
[[Category: Neyer S]]
[[Category: Premkumar L]]