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2yxr

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Current revision (09:10, 25 October 2023) (edit) (undo)
 
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<StructureSection load='2yxr' size='340' side='right'caption='[[2yxr]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='2yxr' size='340' side='right'caption='[[2yxr]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2yxr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YXR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2yxr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YXR FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rhz|1rhz]], [[1rh5|1rh5]], [[2yxq|2yxq]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secY ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067]), secE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067]), secG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yxr OCA], [https://pdbe.org/2yxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yxr RCSB], [https://www.ebi.ac.uk/pdbsum/2yxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yxr ProSAT]</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=2yxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yxr OCA], [https://pdbe.org/2yxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yxr RCSB], [https://www.ebi.ac.uk/pdbsum/2yxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yxr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SECY_METJA SECY_METJA]] 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. [[https://www.uniprot.org/uniprot/SECG_METJA SECG_METJA]] Subunit of the protein translocation channel SecYEG. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. [[https://www.uniprot.org/uniprot/SECE_METJA SECE_METJA]] Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
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[https://www.uniprot.org/uniprot/SECY_METJA SECY_METJA] 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Preprotein translocase|Preprotein translocase]]
*[[Preprotein translocase|Preprotein translocase]]
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*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43067]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, W]]
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[[Category: Methanocaldococcus jannaschii]]
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[[Category: Schulman, S]]
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[[Category: Li W]]
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[[Category: Membrane protein]]
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[[Category: Schulman S]]
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[[Category: Prl mutation]]
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[[Category: Protein secretion]]
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[[Category: Protein translocation]]
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[[Category: Protein transport]]
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[[Category: Signal peptide]]
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[[Category: Translocon]]
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Current revision

The plug domain of the SecY protein stablizes the closed state of the translocation channel and maintains a membrane seal

PDB ID 2yxr

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