3din: Difference between revisions

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<StructureSection load='3din' size='340' side='right'caption='[[3din]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
<StructureSection load='3din' size='340' side='right'caption='[[3din]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3din]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thema Thema] and [https://en.wikipedia.org/wiki/Thesq Thesq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DIN FirstGlance]. <br>
<table><tr><td colspan='2'>[[3din]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8] and [https://en.wikipedia.org/wiki/Thermotoga_sp._RQ2 Thermotoga sp. RQ2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DIN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 4.5&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secA, TM_1578 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), secY, TM_1480 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), secE, TM_0452 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), secG, TRQ2_0456 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=126740 THESQ])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3din FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3din OCA], [https://pdbe.org/3din PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3din RCSB], [https://www.ebi.ac.uk/pdbsum/3din PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3din 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=3din FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3din OCA], [https://pdbe.org/3din PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3din RCSB], [https://www.ebi.ac.uk/pdbsum/3din PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3din ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SECA_THEMA SECA_THEMA]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity). [[https://www.uniprot.org/uniprot/SECE_THEMA SECE_THEMA]] 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_THEMA SECY_THEMA]] 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/SECA_THEMA SECA_THEMA] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thema]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Thesq]]
[[Category: Thermotoga sp. RQ2]]
[[Category: Nam, Y]]
[[Category: Nam Y]]
[[Category: Rapoport, T A]]
[[Category: Rapoport TA]]
[[Category: Zimmer, J]]
[[Category: Zimmer J]]
[[Category: Atp-binding]]
[[Category: Atpase]]
[[Category: Inner membrane]]
[[Category: Membrane protein]]
[[Category: Nucleotide-binding]]
[[Category: Protein translocation]]
[[Category: Protein transport]]
[[Category: Transmembrane]]
[[Category: Transport]]
Retrieved from "https://proteopedia.org/3din"