5o9i

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m (Protected "5o9i" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5o9i is ON HOLD until Paper Publication
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==Crystal structure of transcription factor IIB Mvu mini-intein==
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<StructureSection load='5o9i' size='340' side='right' caption='[[5o9i]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5o9i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O9I FirstGlance]. <br>
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</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=5o9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9i OCA], [http://pdbe.org/5o9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o9i RCSB], [http://www.ebi.ac.uk/pdbsum/5o9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/C9REA0_METVM C9REA0_METVM]] Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).[HAMAP-Rule:MF_00383]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Inteins are mobile genetic elements that are spliced out of proteins after translation. Some inteins contain a homing endonuclease (HEN) responsible for their propagation. Hedgehog/INTein (HINT) domains catalyzing protein splicing and their nested HEN domains are thought to be functionally independent because of the existence of functional mini-inteins without HEN domains. Despite the lack of obvious mutualism between HEN and HINT domains, HEN domains are persistently found at one specific site in inteins, indicating their potential functional role in protein splicing. Here we report crystal structures of inactive and active mini-inteins derived from inteins residing in the transcription factor IIB of Methanococcus jannaschii and Methanocaldococcus vulcanius, revealing a novel modified HINT fold that might provide new insights on the mutualism between the HEN and HINT domains. We propose an evolutionary model of inteins and a functional role of HEN domains in inteins.
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Authors:
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Structural basis for the persistence of homing endonucleases in transcription factor IIB inteins.,Iwai H, Mikula KM, Oeemig JS, Zhou D, Li M, Wlodawer A J Mol Biol. 2017 Oct 18. pii: S0022-2836(17)30498-9. doi:, 10.1016/j.jmb.2017.10.016. PMID:29055778<ref>PMID:29055778</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5o9i" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Iwai, H]]
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[[Category: Li, M]]
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[[Category: Mikula, K M]]
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[[Category: Wlodawer, A]]
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[[Category: Hint fold]]
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[[Category: Mini-intein]]
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[[Category: Transcription]]
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[[Category: Transcription factor iib]]

Revision as of 06:09, 1 November 2017

Crystal structure of transcription factor IIB Mvu mini-intein

5o9i, resolution 2.50Å

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