2fs1: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fs1 OCA], [http://www.ebi.ac.uk/pdbsum/2fs1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fs1 RCSB]</span> | |||
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''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 03:06:55 2008'' | ||
Revision as of 03:06, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
solution structure of PSD-1
OverviewOverview
Protein G-related albumin-binding (GA) modules are frequently expressed on the surfaces of bacterial cells. The limited amino acid sequence variation among GA modules results in structural and functional differences with possible implications for bacterial pathogenesis and host specificity. In particular, the streptococcal G148-GA3 and F. magna ALB8-GA albumin-binding domains exhibit a degree of structural and dynamic diversity that may account for their varied affinities for different species of albumin. To explore the impact of GA module polymorphisms on albumin binding and specificity, we recently used offset recombinant PCR to shuffle seven artificially constructed representatives of the GA sequence space and scan the phage-displayed recombinant domains for mutations that supported binding to the phylogenetically distinct human and guinea pig serum albumins (HSA and GPSA) (Rozak et al. (2006) Biochemistry 45, 3263-3271). Surprisingly, phage selection revealed an overwhelming preference for a single recombinant domain (PSD-1, phage-selected domain-1) regardless of whether the phages were enriched for their abilities to bind one or both of these albumins. We describe here the NMR-derived structure, dynamics, and stability of unbound PSD-1. Our results demonstrate that increased flexibility is not a requirement for broadened specificity, as had been suggested earlier (Johansson et al. (2002) J. Mol. Biol. 316, 1083-1099), because PSD-1 binds the phylogenetically diverse HSA and GPSA even more tightly than G148-GA3 but is less flexible. The structural basis for albumin-binding specificity is analyzed in light of these new results.
About this StructureAbout this Structure
2FS1 is a Protein complex structure of sequences from Peptostreptococcus magnus, streptococcus dysgalactiae, streptococcus equi, streptococcus canis, streptococcus sp.. Full crystallographic information is available from OCA.
ReferenceReference
Structure, dynamics, and stability variation in bacterial albumin binding modules: implications for species specificity., He Y, Rozak DA, Sari N, Chen Y, Bryan P, Orban J, Biochemistry. 2006 Aug 22;45(33):10102-9. PMID:16906768
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