4oz6: Difference between revisions
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''' | ==Structure of the Branched Intermediate in Protein Splicing== | ||
<StructureSection load='4oz6' size='340' side='right' caption='[[4oz6]], [[Resolution|resolution]] 2.79Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oz6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OZ6 OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TIH:BETA(2-THIENYL)ALANINE'>TIH</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<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=4oz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oz6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oz6 RCSB], [http://www.ebi.ac.uk/pdbsum/4oz6 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Inteins are autoprocessing domains that cut themselves out of host proteins in a traceless manner. This process, known as protein splicing, involves multiple chemical steps that must be coordinated to ensure fidelity in the process. The committed step in splicing involves attack of a conserved Asn side-chain amide on the adjacent backbone amide, leading to an intein-succinimide product and scission of that peptide bond. This cleavage reaction is stimulated by formation of a branched intermediate in the splicing process. The mechanism by which the Asn side-chain becomes activated as a nucleophile is not understood. Here we solve the crystal structure of an intein trapped in the branched intermediate step in protein splicing. Guided by this structure, we use protein-engineering approaches to show that intein-succinimide formation is critically dependent on a backbone-to-side-chain hydrogen-bond. We propose that this interaction serves to both position the side-chain amide for attack and to activate its nitrogen as a nucleophile. Collectively, these data provide an unprecedented view of an intein poised to carry out the rate-limiting step in protein splicing, shedding light on how a nominally nonnucleophilic group, a primary amide, can become activated in a protein active site. | |||
Structure of the branched intermediate in protein splicing.,Liu Z, Frutos S, Bick MJ, Vila-Perello M, Debelouchina GT, Darst SA, Muir TW Proc Natl Acad Sci U S A. 2014 Apr 28. PMID:24778214<ref>PMID:24778214</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bick, M J.]] | |||
[[Category: Darst, S A.]] | |||
[[Category: Debelouchina, G T.]] | |||
[[Category: Frutos, S.]] | |||
[[Category: Liu, Z.]] | |||
[[Category: Muir, T W.]] | |||
[[Category: Vila-Perello, M.]] | |||
[[Category: Intein]] | |||
Revision as of 07:18, 14 May 2014
Structure of the Branched Intermediate in Protein Splicing
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