SB2013 L04gr5: Difference between revisions
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=Structure= | =Structure= | ||
The lipoprotein, VlsE, consists of two invariable domains at the amino and carboxyl termini and a variable domain (Figure 1). When referring to the primary structure of the protein, the variable domain is a cassette region located between the two termini. The variable domain can be further broken down into variable regions (<scene name='SB2013_L04gr5/Variable_regions/3'>VRs</scene>) and invariable regions (<scene name='SB2013_L04gr5/Invariable_regions/2'>IRs</scene>) (Liang et al. 1999). When crystallized, VlsE forms a four molecule asymmetric unit (image of the unit) with each molecule having slight differences in their conformation. Although each molecule in the unit is slightly different, a single molecule of the protein consists of eleven [http://en.wikipedia.org/wiki/Alpha_helices α-helices] and four short [http://en.wikipedia.org/wiki/Beta_strand β-strands]. Helices α1 (aa 306-341), α2 (aa 68-87), α3 (aa 114-139), and α11 (aa 306-341) all form the <scene name='SB2013_L04gr5/Membrane_proximal_region/1'>membrane proximal region</scene> of VlsE while helices α4 through α10 form the primary region of the <scene name='SB2013_L04gr5/Membrane_distal_region/2'>membrane distal region</scene> of the protein. The four short β-strands each consist of 3 amino acids and can also be located in the membrane distal region. Covering the membrane distal part of VlsE are connecting loop regions, which lack any secondary structure and have different conformations in each of the molecules. (Eicken et al. 2002). The helices α3 through α10 form the invariable regions and are connected by the connecting loops which are classified as the variable regions. Although VlsE crystallizes into an asymmetrical unit, it appears primarily as monomeric in solution. Because the interface between VlsE molecules in the crystal structure buries approximately 13% of the accessible surface area of the monomers, Eicken et al.suggest that there is a possibility of VlsE existing as a [http://en.wikipedia.org/wiki/Protein_dimer dimer] when in its natural state (Figure 2). <scene name='SB2013_L04gr5/Reset_button/1'>Reset</scene> | The lipoprotein, VlsE, consists of two invariable domains at the amino and carboxyl termini and a variable domain (Figure 1). When referring to the primary structure of the protein, the variable domain is a cassette region located between the two termini. The variable domain can be further broken down into variable regions (<scene name='SB2013_L04gr5/Variable_regions/3'>VRs</scene>) and invariable regions (<scene name='SB2013_L04gr5/Invariable_regions/2'>IRs</scene>) (Liang et al. 1999). When crystallized, VlsE forms a four molecule asymmetric unit (image of the unit) with each molecule having slight differences in their conformation. Although each molecule in the unit is slightly different, a single molecule of the protein consists of eleven [http://en.wikipedia.org/wiki/Alpha_helices α-helices] and four short [http://en.wikipedia.org/wiki/Beta_strand β-strands]. Helices α1 (aa 306-341), α2 (aa 68-87), α3 (aa 114-139), and α11 (aa 306-341) all form the <scene name='SB2013_L04gr5/Membrane_proximal_region/1'>membrane proximal region</scene> of VlsE while helices α4 through α10 form the primary region of the <scene name='SB2013_L04gr5/Membrane_distal_region/2'>membrane distal region</scene> of the protein. The four short β-strands each consist of 3 amino acids and can also be located in the membrane distal region. Covering the membrane distal part of VlsE are connecting loop regions, which lack any secondary structure and have different conformations in each of the molecules. (Eicken et al. 2002). The helices α3 through α10 form the invariable regions and are connected by the connecting loops which are classified as the variable regions. Although VlsE crystallizes into an asymmetrical unit, it appears primarily as monomeric in solution. Because the interface between VlsE molecules in the crystal structure buries approximately 13% of the accessible surface area of the monomers, Eicken et al.suggest that there is a possibility of VlsE existing as a [http://en.wikipedia.org/wiki/Protein_dimer dimer] when in its natural state (Figure 2). <scene name='SB2013_L04gr5/Reset_button/1'>Reset</scene> | ||
[[Image:VlsE 2-d image.jpg]] | [[Image:VlsE 2-d image.jpg]] | ||