3sba: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Zn-mediated Hexamer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization== | ||
<StructureSection load='3sba' size='340' side='right' caption='[[3sba]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3sba]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SBA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sb5|3sb5]], [[3sb6|3sb6]], [[3sb7|3sb7]], [[3sb8|3sb8]], [[3sb9|3sb9]], [[3sbb|3sbb]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=3sba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sba OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sba RCSB], [http://www.ebi.ac.uk/pdbsum/3sba PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Combining the concepts of synthetic symmetrization with the approach of engineering metal binding sites, we have developed a new crystallization methodology termed metal-mediated synthetic symmetrization. In this method, pairs of histidine or cysteine mutations are introduced on the surface of target proteins, generating crystal lattice contacts or oligomeric assemblies upon coordination with metal. Metal-mediated synthetic symmetrization greatly expands the packing and oligomeric assembly possibilities of target proteins, thereby increasing the chances of growing diffraction-quality crystals. To demonstrate this method, we designed various T4 lysozyme (T4L) and maltose-binding protein (MBP) mutants and co-crystallized them with one of three metal ions: copper (Cu(2+) ), nickel (Ni(2+) ) or zinc (Zn(2+) ). The approach resulted in 16 new crystal structures - 8 for T4L and 8 for MBP - displaying a variety of oligomeric assemblies and packing modes, representing in total 13 new and distinct crystal forms for these proteins. We discuss the potential utility of the method for crystallizing target proteins of unknown structure by engineering in pairs of histidine or cysteine residues. As an alternate strategy, we propose that the varied crystallization-prone forms of T4L or MBP engineered in this work could be used as crystallization chaperones, by fusing them genetically to target proteins of interest. | |||
An approach to crystallizing proteins by metal-mediated synthetic symmetrization.,Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO Protein Sci. 2011 Sep 6. doi: 10.1002/pro.727. PMID:21898649<ref>PMID:21898649</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Enterobacteria phage t4]] | [[Category: Enterobacteria phage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Cascio, D | [[Category: Cascio, D]] | ||
[[Category: Laganowsky, A | [[Category: Laganowsky, A]] | ||
[[Category: Sawaya, M R | [[Category: Sawaya, M R]] | ||
[[Category: Soriaga, A B | [[Category: Soriaga, A B]] | ||
[[Category: Yeates, T O | [[Category: Yeates, T O]] | ||
[[Category: Zhao, M | [[Category: Zhao, M]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metal-mediated synthetic symmetrization]] | [[Category: Metal-mediated synthetic symmetrization]] | ||
[[Category: Synthetic symmetrization]] | [[Category: Synthetic symmetrization]] | ||
Revision as of 13:45, 9 December 2014
Zn-mediated Hexamer of T4 Lysozyme R76H/R80H by Synthetic SymmetrizationZn-mediated Hexamer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization
Structural highlights
Publication Abstract from PubMedCombining the concepts of synthetic symmetrization with the approach of engineering metal binding sites, we have developed a new crystallization methodology termed metal-mediated synthetic symmetrization. In this method, pairs of histidine or cysteine mutations are introduced on the surface of target proteins, generating crystal lattice contacts or oligomeric assemblies upon coordination with metal. Metal-mediated synthetic symmetrization greatly expands the packing and oligomeric assembly possibilities of target proteins, thereby increasing the chances of growing diffraction-quality crystals. To demonstrate this method, we designed various T4 lysozyme (T4L) and maltose-binding protein (MBP) mutants and co-crystallized them with one of three metal ions: copper (Cu(2+) ), nickel (Ni(2+) ) or zinc (Zn(2+) ). The approach resulted in 16 new crystal structures - 8 for T4L and 8 for MBP - displaying a variety of oligomeric assemblies and packing modes, representing in total 13 new and distinct crystal forms for these proteins. We discuss the potential utility of the method for crystallizing target proteins of unknown structure by engineering in pairs of histidine or cysteine residues. As an alternate strategy, we propose that the varied crystallization-prone forms of T4L or MBP engineered in this work could be used as crystallization chaperones, by fusing them genetically to target proteins of interest. An approach to crystallizing proteins by metal-mediated synthetic symmetrization.,Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO Protein Sci. 2011 Sep 6. doi: 10.1002/pro.727. PMID:21898649[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||