5jtq: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | {{Large structure}} | ||
==The structure of chaperone SecB in complex with unstructured MBP binding site d== | |||
<StructureSection load='5jtq' size='340' side='right' caption='[[5jtq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jtq]] is a 6 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JTQ FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jtl|5jtl]], [[5jtm|5jtm]], [[5jtn|5jtn]], [[5jto|5jto]], [[5jtp|5jtp]], [[5jtr|5jtr]]</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=5jtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jtq OCA], [http://pdbe.org/5jtq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jtq RCSB], [http://www.ebi.ac.uk/pdbsum/5jtq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jtq ProSAT]</span></td></tr> | |||
</table> | |||
{{Large structure}} | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SECB_ECO57 SECB_ECO57]] One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. [[http://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Molecular chaperones act on non-native proteins in the cell to prevent their aggregation, premature folding or misfolding. Different chaperones often exert distinct effects, such as acceleration or delay of folding, on client proteins via mechanisms that are poorly understood. Here we report the solution structure of SecB, a chaperone that exhibits strong antifolding activity, in complex with alkaline phosphatase and maltose-binding protein captured in their unfolded states. SecB uses long hydrophobic grooves that run around its disk-like shape to recognize and bind to multiple hydrophobic segments across the length of non-native proteins. The multivalent binding mode results in proteins wrapping around SecB. This unique complex architecture alters the kinetics of protein binding to SecB and confers strong antifolding activity on the chaperone. The data show how the different architectures of chaperones result in distinct binding modes with non-native proteins that ultimately define the activity of the chaperone. | |||
Structural basis for the antifolding activity of a molecular chaperone.,Huang C, Rossi P, Saio T, Kalodimos CG Nature. 2016 Aug 8. doi: 10.1038/nature18965. PMID:27501151<ref>PMID:27501151</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5jtq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Huang, C]] | [[Category: Huang, C]] | ||
[[Category: Kalodimos, C G]] | |||
[[Category: Rossi, P]] | [[Category: Rossi, P]] | ||
[[Category: Saio, T]] | [[Category: Saio, T]] | ||
[[Category: | [[Category: Chaperone-protein binding complex]] | ||
[[Category: Molecular chaperone]] | |||
