We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5ch4

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Peptide-Bound State of Thermus thermophilus SecYEG

Structural highlights

5ch4 is a 3 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.64Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SECY_THET8 The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Publication Abstract from PubMed

The bacterial SecYEG translocon functions as a conserved protein-conducting channel. Conformational transitions of SecYEG allow protein translocation across the membrane without perturbation of membrane permeability. Here, we report the crystal structures of intact SecYEG at 2.7-A resolution and of peptide-bound SecYEG at 3.6-A resolution. The higher-resolution structure revealed that the cytoplasmic loop of SecG covers the hourglass-shaped channel, which was confirmed to also occur in the membrane by disulfide bond formation analysis and molecular dynamics simulation. The cytoplasmic loop may be involved in protein translocation. In addition, the previously unknown peptide-bound crystal structure of SecYEG implies that interactions between the cytoplasmic side of SecY and signal peptides are related to lateral gate opening at the first step of protein translocation. These SecYEG structures therefore provide a number of structural insights into the Sec machinery for further study.

Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State.,Tanaka Y, Sugano Y, Takemoto M, Mori T, Furukawa A, Kusakizako T, Kumazaki K, Kashima A, Ishitani R, Sugita Y, Nureki O, Tsukazaki T Cell Rep. 2015 Nov 24;13(8):1561-8. doi: 10.1016/j.celrep.2015.10.025. Epub 2015 , Nov 12. PMID:26586438^[1]

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

References

↑ Tanaka Y, Sugano Y, Takemoto M, Mori T, Furukawa A, Kusakizako T, Kumazaki K, Kashima A, Ishitani R, Sugita Y, Nureki O, Tsukazaki T. Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State. Cell Rep. 2015 Nov 24;13(8):1561-8. doi: 10.1016/j.celrep.2015.10.025. Epub 2015 , Nov 12. PMID:26586438 doi:http://dx.doi.org/10.1016/j.celrep.2015.10.025

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ch4"

@@ Line 1: / Line 1: @@
 ==Peptide-Bound State of Thermus thermophilus SecYEG==
-<StructureSection load='5ch4' size='340' side='right' caption='[[5ch4]], [[Resolution|resolution]] 3.64&Aring;' scene=''>
+<StructureSection load='5ch4' size='340' side='right'caption='[[5ch4]], [[Resolution|resolution]] 3.64&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ch4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CH4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ch4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CH4 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aww|5aww]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.64&#8491;</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=5ch4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ch4 OCA], [http://pdbe.org/5ch4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ch4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ch4 PDBsum]</span></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=5ch4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ch4 OCA], [https://pdbe.org/5ch4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ch4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ch4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ch4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SECY_THET8 SECY_THET8]] The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. [[http://www.uniprot.org/uniprot/SECE_THET8 SECE_THET8]] Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
+[https://www.uniprot.org/uniprot/SECY_THET8 SECY_THET8] The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ishitani, R]]
+[[Category: Large Structures]]
-[[Category: Kumazaki, K]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: Kusakizako, T]]
+[[Category: Ishitani R]]
-[[Category: Nureki, O]]
+[[Category: Kumazaki K]]
-[[Category: Sugano, Y]]
+[[Category: Kusakizako T]]
-[[Category: Takemoto, M]]
+[[Category: Nureki O]]
-[[Category: Tanaka, Y]]
+[[Category: Sugano Y]]
-[[Category: Tsukazaki, T]]
+[[Category: Takemoto M]]
-[[Category: Membrane protein]]
+[[Category: Tanaka Y]]
-[[Category: Protein transport]]
+[[Category: Tsukazaki T]]
-[[Category: Translocon]]

5ch4

From Proteopedia

Current revision

Peptide-Bound State of Thermus thermophilus SecYEG

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox