2aar

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2aar]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AAR FirstGlance]. <br>
<table><tr><td colspan='2'>[[2aar]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AAR FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nkw|1nkw]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nkw|1nkw]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aar OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aar RCSB], [http://www.ebi.ac.uk/pdbsum/2aar PDBsum]</span></td></tr>
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<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=2aar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aar OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aar RCSB], [http://www.ebi.ac.uk/pdbsum/2aar PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TIG_DEIRA TIG_DEIRA]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, PubMed:16271892), exposing a hydrophobic crevice that is probably important for its chaperone activity (PubMed:16091460 and PubMed:16271892).[HAMAP-Rule:MF_00303] [[http://www.uniprot.org/uniprot/RL29_DEIRA RL29_DEIRA]] Binds the 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL23_DEIRA RL23_DEIRA]] One of the early assembly protein (By similarity) it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Forms the main docking site for trigger factor binding to the ribosome (PubMed:16091460 and PubMed:16271892).[HAMAP-Rule:MF_01369]
== 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: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
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[[Category: Auerbach-Nevo, T.]]
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[[Category: Auerbach-Nevo, T]]
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[[Category: Baram, D.]]
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[[Category: Baram, D]]
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[[Category: Bashan, A.]]
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[[Category: Bashan, A]]
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[[Category: Pyetan, E.]]
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[[Category: Pyetan, E]]
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[[Category: Sittner, A.]]
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[[Category: Sittner, A]]
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[[Category: Yonath, A.]]
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[[Category: Yonath, A]]
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[[Category: 50]]
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[[Category: Cheperone]]
[[Category: Cheperone]]
[[Category: Ribosome]]
[[Category: Ribosome]]
[[Category: Trigger factor]]
[[Category: Trigger factor]]
[[Category: Tunnel]]
[[Category: Tunnel]]

Revision as of 20:16, 25 December 2014

Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome.

2aar, resolution 3.50Å

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