4nnj
From Proteopedia
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<StructureSection load='4nnj' size='340' side='right' caption='[[4nnj]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4nnj' size='340' side='right' caption='[[4nnj]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4nnj]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NNJ OCA]. <br> | + | <table><tr><td colspan='2'>[[4nnj]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NNJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NNJ FirstGlance]. <br> |
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| - | <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=4nnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nnj RCSB], [http://www.ebi.ac.uk/pdbsum/4nnj PDBsum]</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=4nnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nnj RCSB], [http://www.ebi.ac.uk/pdbsum/4nnj PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The activation of ubiquitin by the ubiquitin-activating enzyme Uba1 (E1) constitutes the first step in the covalent modification of target proteins with ubiquitin. This activation is a three-step process in which ubiquitin is adenylated at its C-terminal glycine, followed by the covalent attachment of ubiquitin to a catalytic cysteine residue of Uba1 and the subsequent adenylation of a second ubiquitin. Here, a ubiquitin E1 structure loaded with two ubiquitin molecules is presented for the first time. While one ubiquitin is bound in its adenylated form to the active adenylation domain of E1, the second ubiquitin represents the status after transfer and is covalently linked to the active-site cysteine. The covalently linked ubiquitin enables binding of the E2 enzyme without further modification of the ternary Uba1-ubiquitin2 arrangement. This doubly loaded E1 structure constitutes a missing link in the structural analysis of the ubiquitin-transfer cascade. | ||
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| + | Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules.,Schafer A, Kuhn M, Schindelin H Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1311-20. doi:, 10.1107/S1399004714002910. Epub 2014 Apr 30. PMID:24816100<ref>PMID:24816100</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:04, 24 September 2014
Crystal structure of Uba1 in complex with ubiquitin-AMP and thioesterified ubiquitin
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