G09SecL04Tpc2: Difference between revisions
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=== Structural Breakdown === | === Structural Breakdown === | ||
<Structure load='1fj1' size='300' frame='true' align='left' caption='Outer Surface Protein A' scene='G09SecL04Tpc2/Newfirst/1' /> | <Structure load='1fj1' size='300' frame='true' align='left' caption='Outer Surface Protein A' scene='G09SecL04Tpc2/Newfirst/1' /> | ||
<scene name='G09SecL04Tpc2/Newfirst/1'>Reset Model</scene> | |||
Outer Surface Protein A has approximately 270 amino acid residues.<ref name=art3>PMID:11183781</ref> In terms of <scene name='G09SecL04Tpc2/Startospa/3'>secondary structure</scene>, OspA is made up of 21 [http://en.wikipedia.org/wiki/Antiparallel_(biochemistry) anti-parallel] single layer beta strands (gold) and one alpha helix (magenta).<ref name=art3>PMID:11183781</ref> OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/Newfirst/2'>n-terminal sandwich</scene>, central sheet, and a c-terminal barrel domain. 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 <scene name='G09SecL04Tpc2/Newfirst/3'> central beta sheet</scene>. Lastly, the <scene name='G09SecL04Tpc2/Newfirst/4'>c-terminal </scene> is nicknamed barrel domains because the three primary loops on the tip of the c-terminus 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 <scene name='G09SecL04Tpc2/Startospa/3'>secondary structure</scene>, OspA is made up of 21 [http://en.wikipedia.org/wiki/Antiparallel_(biochemistry) anti-parallel] single layer beta strands (gold) and one alpha helix (magenta).<ref name=art3>PMID:11183781</ref> OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/Newfirst/2'>n-terminal sandwich</scene>, central sheet, and a c-terminal barrel domain. 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 <scene name='G09SecL04Tpc2/Newfirst/3'> central beta sheet</scene>. Lastly, the <scene name='G09SecL04Tpc2/Newfirst/4'>c-terminal </scene> is nicknamed barrel domains because the three primary loops on the tip of the c-terminus 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. | ||
