1mi0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mi0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MI0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1mi0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MI0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mhx|1mhx]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mhx|1mhx]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mi0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mi0 PDBsum]</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=1mi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mi0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mi0 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Finegoldia magna]] | [[Category: Finegoldia magna]] | ||
[[Category: Baker, D | [[Category: Baker, D]] | ||
[[Category: Kuhlman, B | [[Category: Kuhlman, B]] | ||
[[Category: Nauli, S | [[Category: Nauli, S]] | ||
[[Category: Stenkamp, R E | [[Category: Stenkamp, R E]] | ||
[[Category: Teller, D C | [[Category: Teller, D C]] | ||
[[Category: Trong, I Le | [[Category: Trong, I Le]] | ||
[[Category: Alpha-beta protein]] | [[Category: Alpha-beta protein]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Redesigned beta-hairpin]] | [[Category: Redesigned beta-hairpin]] | ||
Revision as of 19:12, 5 January 2015
Crystal Structure of the redesigned protein G variant NuG2Crystal Structure of the redesigned protein G variant NuG2
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 PubMedWe recently described two protein G variants (NuG1 and NuG2) with redesigned first hairpins that were almost twice as stable, folded 100-fold faster, and had a switched folding mechanism relative to the wild-type protein. To test the structural accuracy of our design algorithm and to provide insights to the dramatic changes in the kinetics and thermodynamics of folding, we have now determined the crystal structures of NuG1 and NuG2 to 1.8 A and 1.85 A, respectively. We find that they adopt hairpin structures that are closer to the computational models than to wild-type protein G; the RMSD of the NuG1 hairpin to the design model and the wild-type structure are 1.7 A and 5.1 A, respectively. The crystallographic B factor in the redesigned first hairpin of NuG1 is systematically higher than the second hairpin, suggesting that the redesigned region is somewhat less rigid. A second round of structure-based design yielded new variants of NuG1 and NuG2, which are further stabilized by 0.5 kcal/mole and 0.9 kcal/mole. Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2.,Nauli S, Kuhlman B, Le Trong I, Stenkamp RE, Teller D, Baker D Protein Sci. 2002 Dec;11(12):2924-31. PMID:12441390[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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