2hkd
From Proteopedia
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|PDB= 2hkd |SIZE=350|CAPTION= <scene name='initialview01'>2hkd</scene>, resolution 1.60Å | |PDB= 2hkd |SIZE=350|CAPTION= <scene name='initialview01'>2hkd</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene> | + | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | |GENE= ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkd OCA], [http://www.ebi.ac.uk/pdbsum/2hkd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hkd RCSB]</span> | ||
}} | }} | ||
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[[Category: Makabe, K.]] | [[Category: Makabe, K.]] | ||
[[Category: Terechko, V.]] | [[Category: Terechko, V.]] | ||
| - | [[Category: PG4]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
[[Category: engineered protein]] | [[Category: engineered protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:31:36 2008'' |
Revision as of 00:31, 31 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ospA (Borrelia burgdorferi) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of engineered OSPA
Overview
Although the beta-rich self-assemblies are a major structural class for polypeptides and the focus of intense research, little is known about their atomic structures and dynamics due to their insoluble and noncrystalline nature. We developed a protein engineering strategy that captures a self-assembly segment in a water-soluble molecule. A predefined number of self-assembling peptide units are linked, and the beta-sheet ends are capped to prevent aggregation, which yields a mono-dispersed soluble protein. We tested this strategy by using Borrelia outer surface protein (OspA) whose single-layer beta-sheet located between two globular domains consists of two beta-hairpin units and thus can be considered as a prototype of self-assembly. We constructed self-assembly mimics of different sizes and determined their atomic structures using x-ray crystallography and NMR spectroscopy. Highly regular beta-sheet geometries were maintained in these structures, and peptide units had a nearly identical conformation, supporting the concept that a peptide in the regular beta-geometry is primed for self-assembly. However, we found small but significant differences in the relative orientation between adjacent peptide units in terms of beta-sheet twist and bend, suggesting their inherent flexibility. Modeling shows how this conformational diversity, when propagated over a large number of peptide units, can lead to a substantial degree of nanoscale polymorphism of self-assemblies.
About this Structure
2HKD is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.
Reference
Atomic structures of peptide self-assembly mimics., Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:17093048
Page seeded by OCA on Mon Mar 31 03:31:36 2008
