4v4n: Difference between revisions
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<StructureSection load='4v4n' size='340' side='right' caption='[[4v4n]], [[Resolution|resolution]] 9.00Å' scene=''> | <StructureSection load='4v4n' size='340' side='right' caption='[[4v4n]], [[Resolution|resolution]] 9.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v4n]] is a 69 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entries | <table><tr><td colspan='2'>[[4v4n]] is a 69 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j43 3j43], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j44 3j44] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vvk 1vvk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V4N FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j43|3j43]], [[3j44|3j44]], [[1vvk|1vvk]], [[3j21|3j21]], [[3j2l|3j2l]], [[3j20|3j20]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j43|3j43]], [[3j44|3j44]], [[1vvk|1vvk]], [[3j21|3j21]], [[3j2l|3j2l]], [[3j20|3j20]]</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=4v4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v4n RCSB], [http://www.ebi.ac.uk/pdbsum/4v4n PDBsum]</span></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=4v4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v4n RCSB], [http://www.ebi.ac.uk/pdbsum/4v4n PDBsum]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | |||
== Function == | == Function == | ||
[[http://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. [[http://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. [[http://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. | [[http://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. [[http://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. [[http://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. | ||