3cmm

<StructureSection load='3cmm' size='340' side='right' caption='[[3cmm]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[3cmm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CMM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), UBI1, RPL40A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=3cmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cmm OCA], [http://pdbe.org/3cmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cmm RCSB], [http://www.ebi.ac.uk/pdbsum/3cmm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cmm ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/UBA1_YEAST UBA1_YEAST]] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/3cmm_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes of enzymes, E1, E2, and E3. Each E1 adenylates the C terminus of its cognate Ubl, forms a E1 approximately Ubl thioester intermediate, and ultimately generates a thioester-linked E2 approximately Ubl product. We have determined the crystal structure of yeast Uba1, revealing a modular architecture with individual domains primarily mediating these specific activities. The negatively charged C-terminal ubiquitin-fold domain (UFD) is primed for binding of E2s and recognizes their positively charged first alpha helix via electrostatic interactions. In addition, a mobile loop from the domain harboring the E1 catalytic cysteine contributes to E2 binding. Significant, experimentally observed motions in the UFD around a hinge in the linker connecting this domain to the rest of the enzyme suggest a conformation-dependent mechanism for the transthioesterification function of Uba1; however, this mechanism clearly differs from that of other E1 enzymes.

Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes.,Lee I, Schindelin H Cell. 2008 Jul 25;134(2):268-78. PMID:18662542<ref>PMID:18662542</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3cmm" style="background-color:#fffaf0;"></div>

*[[Ubiquitin|Ubiquitin]]

*[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]]

[[Category: Lee, I]]

[[Category: Schindelin, H]]

[[Category: Ubl conjugation pathway]]