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| | ==Crystal structure of SAMP1 from Haloferax volcanii== | | ==Crystal structure of SAMP1 from Haloferax volcanii== |
| - | <StructureSection load='3po0' size='340' side='right' caption='[[3po0]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='3po0' size='340' side='right'caption='[[3po0]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3po0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halvd Halvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PO0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3po0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halvd Halvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PO0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3po0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3po0 OCA], [http://pdbe.org/3po0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3po0 RCSB], [http://www.ebi.ac.uk/pdbsum/3po0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3po0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3po0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3po0 OCA], [https://pdbe.org/3po0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3po0 RCSB], [https://www.ebi.ac.uk/pdbsum/3po0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3po0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SAMP1_HALVD SAMP1_HALVD]] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. | + | [[https://www.uniprot.org/uniprot/SAMP1_HALVD SAMP1_HALVD]] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Halvd]] | | [[Category: Halvd]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Jeong, B C]] | | [[Category: Jeong, B C]] |
| | [[Category: Jeong, Y J]] | | [[Category: Jeong, Y J]] |
| Structural highlights
Function
[SAMP1_HALVD] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation.
Publication Abstract from PubMed
The ubiquitin-like (Ubl) system has been shown to be ubiquitous in all three kingdoms of life following the very recent characterization of ubiquitin-like small archaeal modifier proteins (SAMP1 and 2) from Haloferax volcanii. The ubiquitin (Ub) and Ubl molecules in eukaryotes have been studied extensively and their cellular functions are well established. Biochemical and structural data pertaining to prokaryotic Ubl protein (Pup) continue to be reported. In contrast to eukaryotes and prokaryotes, no structural information on the archaeal Ubl molecule is available. Here we determined the crystal structure of SAMP1 at 1.55A resolution and generated a model of SAMP2. These were then compared with other Ubl molecules from eukaryotes as well as prokaryotes. The structure of SAMP1 shows a beta-grasp fold of Ub, suggesting that the archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. The current structure identifies the location of critical elements such a single lysine residue (Lys4), C-terminal di-glycine motif, hydrophobic patches near leucine 60, and uniquely inserted alpha-helical segments (alpha1 and alpha3) in SAMP1. Based on the structure of SAMP1, several Ub-like features of SAMPs such as poly-SAMPylation and non-covalent interactions have been proposed, which should provide the basis for further investigations concerning the molecular function of archaeal Ubls and the large super-family of beta-grasp fold proteins in the archaeal kingdom.
Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii.,Jeong YJ, Jeong BC, Song HK Biochem Biophys Res Commun. 2011 Feb 4;405(1):112-7. Epub 2011 Jan 7. PMID:21216237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jeong YJ, Jeong BC, Song HK. Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii. Biochem Biophys Res Commun. 2011 Feb 4;405(1):112-7. Epub 2011 Jan 7. PMID:21216237 doi:10.1016/j.bbrc.2011.01.004
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