4do2
From Proteopedia
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| - | [[ | + | ==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.== |
| + | <StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4do2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DO2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rop|1rop]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rop ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [http://www.ebi.ac.uk/pdbsum/4do2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region has attracted considerable interest because a single alanine-to-proline substitution (A31P) in the loop is sufficient to change the topology of this small protein. In order to further analyse the loop region as a possible folding-control element, the double mutant D30P/A31G (RopPG) was produced, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 26.7, b = 38.8, c = 56.6 A, beta = 100.9 degrees and two molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 1.4 A using synchrotron radiation. | ||
| - | + | Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.,Ambrazi M, Fellas G, Kapetaniou EG, Kotsifaki D, Providaki M, Kokkinidis M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):432-4. doi:, 10.1107/S1744309108011342. Epub 2008 Apr 30. PMID:18453719<ref>PMID:18453719</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Rop protein|Rop protein]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Amprazi, M | + | [[Category: Amprazi, M]] |
| - | [[Category: Kapetaniou, E G | + | [[Category: Kapetaniou, E G]] |
| - | [[Category: M., Kokkinidis | + | [[Category: M., Kokkinidis]] |
[[Category: 4-alpha-helical bundle]] | [[Category: 4-alpha-helical bundle]] | ||
[[Category: Bacterial protein]] | [[Category: Bacterial protein]] | ||
Revision as of 17:13, 9 December 2014
Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.
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