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| | <StructureSection load='5l8z' size='340' side='right'caption='[[5l8z]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='5l8z' size='340' side='right'caption='[[5l8z]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l8z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiroplasma_melliferum_kc3 Spiroplasma melliferum kc3]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5cvx 5cvx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L8Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5L8Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l8z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiroplasma_melliferum_KC3 Spiroplasma melliferum KC3]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4n1v 4n1v] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5cvx 5cvx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L8Z FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPM_000560 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=570509 Spiroplasma melliferum KC3])</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=5l8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l8z OCA], [https://pdbe.org/5l8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l8z RCSB], [https://www.ebi.ac.uk/pdbsum/5l8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l8z ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5l8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l8z OCA], [http://pdbe.org/5l8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l8z RCSB], [http://www.ebi.ac.uk/pdbsum/5l8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l8z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A037USE5_SPIME A0A037USE5_SPIME] |
| | <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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Spiroplasma melliferum kc3]] | + | [[Category: Spiroplasma melliferum KC3]] |
| - | [[Category: Boyko, K M]] | + | [[Category: Boyko KM]] |
| - | [[Category: Gorbacheva, M A]] | + | [[Category: Gorbacheva MA]] |
| - | [[Category: Kamashev, D E]] | + | [[Category: Kamashev DE]] |
| - | [[Category: Korzhenevskiy, D A]] | + | [[Category: Korzhenevskiy DA]] |
| - | [[Category: Lipkin, A V]] | + | [[Category: Lipkin AV]] |
| - | [[Category: Popov, V O]] | + | [[Category: Popov VO]] |
| - | [[Category: Rakitina, T V]] | + | [[Category: Rakitina TV]] |
| - | [[Category: Vanyushkina, A A]] | + | [[Category: Vanyushkina AA]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Histone-like]]
| + | |
| - | [[Category: Hu-protein]]
| + | |
| - | [[Category: Nap]]
| + | |
| - | [[Category: Spiroplasma melliferum]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| Structural highlights
Function
A0A037USE5_SPIME
Publication Abstract from PubMed
The three-dimensional structure of the histone-like HU protein from the mycoplasma Spiroplasma melliferum KC3 (HUSpm) was determined at 1.4 A resolution, and the thermal stability of the protein was evaluated by differential scanning calorimetry. A detailed analysis revealed that the three-dimensional structure of the HUSpm dimer is similar to that of its bacterial homologues but is characterized by stronger hydrophobic interactions at the dimer interface. This HUSpm dimer interface lacks salt bridges but is stabilized by a larger number of hydrogen bonds. According to the DSC data, HUSpm has a high denaturation temperature, comparable to that of HU proteins from thermophilic bacteria. To elucidate the structural basis of HUSpm thermal stability, we identified amino acid residues potentially responsible for this property and modified them by site-directed mutagenesis. A comparative analysis of the melting curves of mutant and wild-type HUSpm revealed the motifs that play a key role in protein thermal stability: non-conserved phenylalanine residues in the hydrophobic core, an additional hydrophobic loop at the N-terminal region of the protein, the absence of the internal cavity present at the dimer interface of some HU proteins, and the presence of additional hydrogen bonds between the monomers that are missing in homologous proteins.
Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3.,Boyko KM, Rakitina TV, Korzhenevskiy DA, Vlaskina AV, Agapova YK, Kamashev DE, Kleymenov SY, Popov VO Sci Rep. 2016 Nov 3;6:36366. doi: 10.1038/srep36366. PMID:27808161[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyko KM, Rakitina TV, Korzhenevskiy DA, Vlaskina AV, Agapova YK, Kamashev DE, Kleymenov SY, Popov VO. Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3. Sci Rep. 2016 Nov 3;6:36366. doi: 10.1038/srep36366. PMID:27808161 doi:http://dx.doi.org/10.1038/srep36366
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