This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5y82

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:12, 21 October 2020

Crystal structure of the periplasmic domain of the Thermotoga maritima YidC

Structural highlights

5y82 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[YIDC_THEMA] Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.

Publication Abstract from PubMed

The evolutionarily conserved YidC/Oxa1/Alb3 family of proteins represents a unique membrane protein family that facilitates the insertion, folding, and assembly of a cohort of alpha-helical membrane proteins in all kingdoms of life, yet its underlying mechanisms remain elusive. We report the crystal structures of the full-length Thermotoga maritima YidC (TmYidC) and the TmYidC periplasmic domain (TmPD) at a resolution of 3.8 and 2.5 A, respectively. The crystal structure of TmPD reveals a beta-supersandwich fold but with apparently shortened beta strands and different connectivity, as compared to the Escherichia coli YidC (EcYidC) periplasmic domain (EcPD). TmYidC in a detergent-solubilized state also adopts a monomeric form and its conserved core domain, which consists of 2 loosely associated alpha-helical bundles, assemble a fold similar to that of the other YidC homologues, yet distinct from that of the archaeal YidC-like DUF106 protein. Functional analysis using in vivo photo-crosslinking experiments demonstrates that Pf3 coat protein, a Sec-independent YidC substrate, exits to the lipid bilayer laterally via one of the 2 alpha-helical bundle interfaces: TM3-TM5. Engineered intramolecular disulfide bonds in TmYidC, in combination with complementation assays, suggest that significant rearrangement of the 2 alpha-helical bundles at the top of the hydrophilic groove is critical for TmYidC function. These experiments provide a more detailed mechanical insight into YidC-mediated membrane protein biogenesis.-Xin, Y., Zhao, Y., Zheng, J., Zhou, H., Zhang, X. C., Tian, C., Huang, Y. Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion.

Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion.,Xin Y, Zhao Y, Zheng J, Zhou H, Zhang XC, Tian C, Huang Y FASEB J. 2018 May;32(5):2411-2421. doi: 10.1096/fj.201700893RR. Epub 2018 Jan 2. PMID:29295859^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xin Y, Zhao Y, Zheng J, Zhou H, Zhang XC, Tian C, Huang Y. Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion. FASEB J. 2018 May;32(5):2411-2421. doi: 10.1096/fj.201700893RR. Epub 2018 Jan 2. PMID:29295859 doi:http://dx.doi.org/10.1096/fj.201700893RR

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5y82"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the periplasmic domain of the Thermotoga maritima YidC==
-<StructureSection load='5y82' size='340' side='right' caption='[[5y82]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
+<StructureSection load='5y82' size='340' side='right'caption='[[5y82]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5y82]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y82 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5y82]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y82 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5Y82 FirstGlance]. <br>
-</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=5y82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y82 OCA], [http://pdbe.org/5y82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y82 RCSB], [http://www.ebi.ac.uk/pdbsum/5y82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y82 ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5y82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y82 OCA], [http://pdbe.org/5y82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y82 RCSB], [http://www.ebi.ac.uk/pdbsum/5y82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y82 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
 </div>
 <div class="pdbe-citations 5y82" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Insertase|Insertase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Huang, Y]]
 [[Category: Xin, Y]]

5y82

From Proteopedia

Revision as of 09:12, 21 October 2020

Crystal structure of the periplasmic domain of the Thermotoga maritima YidC

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox