2l52
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans== |
| + | <StructureSection load='2l52' size='340' side='right' caption='[[2l52]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2l52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L52 FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">moaD, MA_4086 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2214 Methanosarcina acetivorans])</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=2l52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l52 RCSB], [http://www.ebi.ac.uk/pdbsum/2l52 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In archaea, two ubiquitin-like small archaeal modifier protein (SAMPs) were recently shown to be conjugated to proteins in vivo. SAMPs display homology to bacterial MoaD sulfur transfer proteins and eukaryotic ubiquitin-like proteins, and they share with them the conserved C-terminal glycine-glycine motif. Here, we report the solution structure of SAMP1 from Methanosarcina acetivorans and the activation of SAMPs by an archaeal protein with homology to eukaryotic E1 enzymes. Our results show that SAMP1 possesses a beta-grasp fold and that its hydrophobic and electrostatic surface features are similar to those of MoaD. M. acetivorans SAMP1 exhibits an extensive flexible surface loop between helix-2 and the third strand of the beta-sheet, which contributes to an elongated surface groove that is not observed in bacterial ubiquitin homologues and many other SAMPs. We provide in vitro biochemical evidence that SAMPs are activated in an ATP-dependent manner by an E1-like enzyme that we have termed E1-like SAMP activator (ELSA). We show that activation occurs by formation of a mixed anhydride (adenylate) at the SAMP C-terminus and is detectable by SDS-PAGE and electrospray ionization mass spectrometry. | ||
| - | + | Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins.,Ranjan N, Damberger FF, Sutter M, Allain FH, Weber-Ban E J Mol Biol. 2011 Jan 28;405(4):1040-55. Epub 2010 Nov 26. PMID:21112336<ref>PMID:21112336</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Methanosarcina acetivorans]] | [[Category: Methanosarcina acetivorans]] | ||
[[Category: Allain, F H.T.]] | [[Category: Allain, F H.T.]] | ||
Revision as of 11:27, 20 October 2014
Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans
| |||||||||||
