3wvf: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Crystal structure of YidC from Escherichia coli==

== Structural highlights ==

<table><tr><td colspan='2'>[[3wvf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WVF 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=3wvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wvf RCSB], [http://www.ebi.ac.uk/pdbsum/3wvf PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophilic groove, formed by five transmembrane helices, is a conserved structural feature of YidC, as compared to the previous YidC structure from Bacillus halodurans, which lacks a periplasmic domain. Structural mapping of the substrate- or Sec protein-contact sites suggested the importance of the groove for the YidC functions as a chaperone and an insertase, and provided structural insight into the multi-protein complex.

~~The entry 3wvf is ON HOLD until Paper Publication~~

Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.,Kumazaki K, Kishimoto T, Furukawa A, Mori H, Tanaka Y, Dohmae N, Ishitani R, Tsukazaki T, Nureki O Sci Rep. 2014 Dec 3;4:7299. doi: 10.1038/srep07299. PMID:25466392<ref>PMID:25466392</ref>

~~Authors: Kumazaki~~, K.~~, Tsukazaki, T~~., Kishimoto, T~~., Ishitani, R.~~, Nureki, O.

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

</div>

~~Description~~:

== References ==

__TOC__

</StructureSection>

[[Category: Ishitani, R]]

[[Category: Kishimoto, T]]

[[Category: Kumazaki, K]]

[[Category: Nureki, O]]

[[Category: Tsukazaki, T]]

[[Category: Alpha helical]]

[[Category: Chaperone]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of YidC from Escherichia coli==
+<StructureSection load='3wvf' size='340' side='right' caption='[[3wvf]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3wvf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WVF 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=3wvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wvf RCSB], [http://www.ebi.ac.uk/pdbsum/3wvf PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophilic groove, formed by five transmembrane helices, is a conserved structural feature of YidC, as compared to the previous YidC structure from Bacillus halodurans, which lacks a periplasmic domain. Structural mapping of the substrate- or Sec protein-contact sites suggested the importance of the groove for the YidC functions as a chaperone and an insertase, and provided structural insight into the multi-protein complex.
-The entry 3wvf is ON HOLD  until Paper Publication
+Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.,Kumazaki K, Kishimoto T, Furukawa A, Mori H, Tanaka Y, Dohmae N, Ishitani R, Tsukazaki T, Nureki O Sci Rep. 2014 Dec 3;4:7299. doi: 10.1038/srep07299. PMID:25466392<ref>PMID:25466392</ref>
-Authors: Kumazaki, K., Tsukazaki, T., Kishimoto, T., Ishitani, R., Nureki, O.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Ishitani, R]]
+[[Category: Kishimoto, T]]
+[[Category: Kumazaki, K]]
+[[Category: Nureki, O]]
+[[Category: Tsukazaki, T]]
+[[Category: Alpha helical]]
+[[Category: Chaperone]]