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Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices

by Robinette, Rebekah A , Deivanayagam, Champion , Rajashankar, Kanagalaghatta R , Patel, Manisha H , Crowley, Paula J , Brady, L Jeannine , Michalek, Suzanne , Larson, Matthew R

in AGGLUTININS / ANTIGENS / ARCHITECTURE / Binding sites / CALORIMETRY / CRYSTAL STRUCTURE / MATERIALS SCIENCE / PLASMONS / PROTEIN STRUCTURE / PROTEINS / RESONANCE / SEDIMENTATION / STREPTOCOCCUS / Streptococcus infections / TITRATION / VELOCITY / VIRULENCE

2010

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Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices

by Robinette, Rebekah A , Deivanayagam, Champion , Rajashankar, Kanagalaghatta R , Patel, Manisha H , Crowley, Paula J , Brady, L Jeannine , Michalek, Suzanne , Larson, Matthew R

2010

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Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices

by Robinette, Rebekah A , Deivanayagam, Champion , Rajashankar, Kanagalaghatta R , Patel, Manisha H , Crowley, Paula J , Brady, L Jeannine , Michalek, Suzanne , Larson, Matthew R

2010

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Journal Article

Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices

Robinette, Rebekah A,

Deivanayagam, Champion,

Rajashankar, Kanagalaghatta R,

Patel, Manisha H,

Crowley, Paula J,

Brady, L Jeannine,

Michalek, Suzanne,

Larson, Matthew R

2010

Overview

Streptococcus mutans antigen I/II (AgI/II) is a cell surface-localized protein adhesin that interacts with salivary components within the salivary pellicle. AgI/II contributes to virulence and has been studied as an immunological and structural target, but a fundamental understanding of its underlying architecture has been lacking. Here we report a high-resolution (1.8 A) crystal structure of the A...VP... fragment of S. mutans AgI/II that demonstrates a unique fibrillar form (155 A) through the interaction of two noncontiguous regions in the primary sequence. The A... repeat of the alanine-rich domain adopts an extended α-helix that intertwines with the P... repeat polyproline type II (PPII) helix to form a highly extended stalk-like structure heretofore unseen in prokaryotic or eukaryotic protein structures. Velocity sedimentation studies indicate that full-length AgI/II that contains three A/P repeats extends over 50 nanometers in length. Isothermal titration calorimetry revealed that the high-affinity association between the A... and P... helices is enthalpically driven. Two distinct binding sites on AgI/II to the host receptor salivary agglutinin (SAG) were identified by surface plasmon resonance (SPR). The current crystal structure reveals that AgI/II family proteins are extended fibrillar structures with the number of alanine- and proline-rich repeats determining their length. (ProQuest: ... denotes formulae/symbols omitted.)

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National Academy of Sciences

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