2zd0: Difference between revisions
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==Crystal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP)== | |||
<StructureSection load='2zd0' size='340' side='right' caption='[[2zd0]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2zd0' size='340' side='right' caption='[[2zd0]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zd0]] is a 3 chain structure | <table><tr><td colspan='2'>[[2zd0]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZD0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2exs|2exs]], [[2ext|2ext]], [[1qaw|1qaw]], [[2zcz|2zcz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2exs|2exs]], [[2ext|2ext]], [[1qaw|1qaw]], [[2zcz|2zcz]]</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=2zd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd0 OCA], [http://pdbe.org/2zd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zd0 RCSB], [http://www.ebi.ac.uk/pdbsum/2zd0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zd0 ProSAT]</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=2zd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd0 OCA], [http://pdbe.org/2zd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zd0 RCSB], [http://www.ebi.ac.uk/pdbsum/2zd0 PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Heddle, J G]] | [[Category: Heddle, J G]] | ||
[[Category: Mishima, Y]] | [[Category: Mishima, Y]] | ||
Revision as of 10:00, 9 March 2017
Crystal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP)Crystal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP)
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe ability of proteins to self-assemble into complex, functional nanoscale structures is expected to become of significant use in the manufacture of artificial nanodevices with a wide range of novel applications. The bacterial protein TRAP has potential uses as a nanoscale component as it is ring-shaped, with a central, modifiable cavity. Furthermore, it can be engineered to make a ring of 12-fold symmetry, which is advantageous for packing into two-dimensional arrays. The 12mer form of TRAP is made by linking multiple subunits together on the same polypeptide, but the usefulness of the 12mers described to date is limited by their poor stability. Here we show that, by altering the length of the peptide linker between subunits, the thermostability can be significantly improved. Since the subunit interfaces of the different 12mers are essentially identical, stabilization arises from the reduction of strain in the linkers. Such a simple method of controlling the stability of modular proteins may have wide applications, and demonstrates the lack of absolute correlation between interactions observable by crystallography and the internal energy of a complex. Intersubunit linker length as a modifier of protein stability: crystal structures and thermostability of mutant TRAP.,Watanabe M, Mishima Y, Yamashita I, Park SY, Tame JR, Heddle JG Protein Sci. 2008 Mar;17(3):518-26. PMID:18287284[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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