SB2013 L08gr01: Difference between revisions
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==OspC Structure== | ==OspC Structure== | ||
{{STRUCTURE_1ggq | PDB=1ggq}} | {{STRUCTURE_1ggq | PDB=1ggq}} | ||
The highly variable OspC gene is located on a 27 kb circular plasmid and encodes for lipoprotein, which contains an 18 amino acid sequence. This amino acid sequence changes after processing and lipidation at the amino proximal Cys residue. The high variability of OspC gene makes OspC protein very polymorphic which varies among the major groups and even within different locations (Kumaran et al. 2001). It is also important to note that there is a high variance in the amino acid sequence of the invasive <scene name='Talk:SB2013_L08gr1/Amino_sequence/1'>putative site</scene> from non-invasive species, contributing to the differentiation of folding and solvent structures of putative sites. The three dimensional <scene name='colorSTRUCTURE'>structure</scene> of OspC consists of five helices and two anti-parallel beta sheets per monomer (Figure 1). Not all strains of OspC are invasive to humans (less than half). Even within invasive groups, the amino acid sequence varies (dissimilarity in building units), yet all of the invasive groups continue to share remarkably well reserved solvent structures (Figure 5) within the cavity (similarity in 3D structure and folding leading to a similar function). Another point of significance to be added is that regions in all invasive species are likely to be partially occupied by heavy trace ions (Kumaran et al. 2001).One of the most prominent differences between OspC of invasive species and that of a non-invasive species is that OspC found on invasive strands of spirochetes has a strong negative electrostatic potential region which exists within its two-fold axis (Figure 2). | The highly variable OspC gene is located on a 27 kb circular plasmid and encodes for lipoprotein, which contains an 18 amino acid sequence. This amino acid sequence changes after processing and lipidation at the amino proximal Cys residue. The high variability of OspC gene makes OspC protein very polymorphic which varies among the major groups and even within different locations (Kumaran et al. 2001). It is also important to note that there is a high variance in the amino acid sequence of the invasive <scene name='Talk:SB2013_L08gr1/Amino_sequence/1'>putative site</scene> from non-invasive species, contributing to the differentiation of folding and solvent structures of putative sites. The three dimensional <scene name='colorSTRUCTURE'>structure</scene> of OspC consists of five helices and two anti-parallel beta sheets per monomer (Figure 1). Not all strains of OspC are invasive to humans (less than half). Even within invasive groups, the amino acid sequence varies (dissimilarity in building units), yet all of the invasive groups continue to share remarkably well reserved solvent structures (Figure 5) within the cavity (similarity in 3D structure and folding leading to a similar function). Another point of significance to be added is that regions in all invasive species are likely to be partially occupied by heavy trace ions (Kumaran et al. 2001).One of the most prominent differences between OspC of invasive species and that of a non-invasive species is that OspC found on invasive strands of spirochetes has a strong negative electrostatic potential region which exists within its two-fold axis (Figure 2). | ||
[[Image:Electronegativity of OspC.jpg]] | |||
==Structural Function== | ==Structural Function== | ||