G09SecL04Tpc2: Difference between revisions

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== Outer Surface Protein A (OspA) ==
== Outer Surface Protein A (OspA) ==
=== Structural Breakdown ===
<Structure load='1fj1' size='350' frame='true' align='right' caption='Outer Surface Protein A' scene='G09SecL04Tpc2/Startospa/3' />
<Structure load='1fj1' size='350' frame='true' align='right' caption='Outer Surface Protein A' scene='G09SecL04Tpc2/Startospa/3' />
<scene name='G09SecL04Tpc2/Startospa/3'>Reset Model</scene>
<scene name='G09SecL04Tpc2/Startospa/3'>Reset Model</scene>


=== Structural Breakdown ===
Outer Surface Protein A has approximately 270 amino acid residues. <ref name=art3>PMID:11183781</ref>In terms of secondary structure, OspA is made up of 21 anti-parallel single layer beta strands and one alpha helix. <ref name=art3>PMID:11183781</ref>OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/3sites/3'>n-terminal sandwich</scene>, <scene name='G09SecL04Tpc2/3sites/2'>a central sheet</scene>, and a <scene name='G09SecL04Tpc2/3sites/4'>c-terminal barrel domain</scene>. The n-terminal is often termed as a sandwich due to its jumbled formation of amino acid residues. Most of the beta strands lie on the central sheet. Lastly, the c-terminal is called barrel domains because the three primary loops connect to both sides of the central beta sheet forming a barrel or a hole in the middle. This can be seen by rotating the molecule.  
Outer Surface Protein A has approximately 270 amino acid residues. <ref name=art3>PMID:11183781</ref>In terms of secondary structure, OspA is made up of 21 anti-parallel single layer beta strands and one alpha helix. <ref name=art3>PMID:11183781</ref>OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/3sites/3'>n-terminal sandwich</scene>, <scene name='G09SecL04Tpc2/3sites/2'>a central sheet</scene>, and a <scene name='G09SecL04Tpc2/3sites/4'>c-terminal barrel domain</scene>. The n-terminal is often termed as a sandwich due to its jumbled formation of amino acid residues. Most of the beta strands lie on the central sheet. Lastly, the c-terminal is called barrel domains because the three primary loops connect to both sides of the central beta sheet forming a barrel or a hole in the middle. This can be seen by rotating the molecule.