2l0m

<StructureSection load='2l0m' size='340' side='right' caption='[[2l0m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2l0m]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L0M FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zuq|2zuq]], [[2k73|2k73]]</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=2l0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0m OCA], [http://pdbe.org/2l0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l0m RCSB], [http://www.ebi.ac.uk/pdbsum/2l0m PDBsum]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/C4ZTM6_ECOBW C4ZTM6_ECOBW]] Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.[HAMAP-Rule:MF_00286]

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== Publication Abstract from PubMed ==

The two-stage model for membrane protein folding postulates that individual helices form first and are subsequently packed against each other. To probe the two-stage model, the structures of peptides representing individual transmembrane helices of the disulfide bond forming protein B have been studied in trifluoroethanol solution as well as in detergent micelles using nuclear magnetic resonance (NMR) and circular dichroism spectroscopy. In TFE solution, peptides showed well-defined alpha-helical structures. Peptide structures in TFE were compared to the structures of full-length protein obtained by X-ray crystallography and NMR. The extent of alpha-helical secondary structure coincided well, lending support for the two-stage model for membrane protein folding. However, the conformation of some amino acid side chains differs between the structures of peptide and full-length protein. In micellar solution, the peptides also adopted a helical structure, albeit of reduced definition. Using measurements of paramagnetic relaxation enhancement, peptides were confirmed to be embedded in micelles. These observations may indicate that in the native protein, tertiary interactions additionally stabilize the secondary structure of the individual transmembrane helices. Proteins 2011. (c) 2011 Wiley-Liss, Inc.

Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy.,Hwang S, Hilty C Proteins. 2011 Jan 4. doi: 10.1002/prot.22877. PMID:21337621<ref>PMID:21337621</ref>

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

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<div class="pdbe-citations 2l0m" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hilty, C]]

[[Category: Hwang, S]]

[[Category: Dsbb]]

[[Category: Folding]]

[[Category: Organic solvent]]