Journal:Acta Cryst F:S2053230X19004151
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 8: | Line 8: | ||
The crystallization conditions, data collection strategies, and structure determination methods used on five sections that together make up >90% of a 1.5-megadalton ice-binding adhesin protein, MpIBP, were described. This enormous adhesin is expressed on the exterior surface of the Gram-negative marine bacterium ''Marinomonas primoryensis'', where it contributes to the bacterium’s ability to bind surface ice in an Antarctic lake for better access to oxygen and nutrients. It is hypothesized that this surface protein uses > 600 Ca2+ to help rigidify the chain formed by one of its domains repeated ~120 times in tandem in region II (RII), and to aid in proper folding and function of domains in the other regions (RI, RIII, RIV, and RV). Here, natural incorporation of Ca2+ within the protein scaffold, as occurs in an abundance of proteins, presented a straightforward path to obtain needed phasing information for ''de novo'' protein structure determination. | The crystallization conditions, data collection strategies, and structure determination methods used on five sections that together make up >90% of a 1.5-megadalton ice-binding adhesin protein, MpIBP, were described. This enormous adhesin is expressed on the exterior surface of the Gram-negative marine bacterium ''Marinomonas primoryensis'', where it contributes to the bacterium’s ability to bind surface ice in an Antarctic lake for better access to oxygen and nutrients. It is hypothesized that this surface protein uses > 600 Ca2+ to help rigidify the chain formed by one of its domains repeated ~120 times in tandem in region II (RII), and to aid in proper folding and function of domains in the other regions (RI, RIII, RIV, and RV). Here, natural incorporation of Ca2+ within the protein scaffold, as occurs in an abundance of proteins, presented a straightforward path to obtain needed phasing information for ''de novo'' protein structure determination. | ||
| - | X-ray crystal structures | + | X-ray crystal structures: |
| - | *<scene name='81/812834/Cv/4'>RII-monomer</scene> (PDB [[4kdv]]; cyan). | + | *<scene name='81/812834/Cv/4'>RII-monomer</scene> (PDB [[4kdv]]; cyan). Ca2+ are shown as green spheres. |
| + | *<scene name='81/812834/Cvx/4'>RIII_1-2</scene> (blue). | ||
| + | *<scene name='81/812834/Cvx/5'>RIII_1-4</scene> (PDB [[5k8g]]; blue). | ||
*<scene name='81/812834/Cv/3'>RIII_5</scene> (PDB [[5j6y]]; seagreen). | *<scene name='81/812834/Cv/3'>RIII_5</scene> (PDB [[5j6y]]; seagreen). | ||
*<scene name='81/812834/Cvx/3'>RV</scene> (PDB [[5juh]]; magenta). | *<scene name='81/812834/Cvx/3'>RV</scene> (PDB [[5juh]]; magenta). | ||
Current revision
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
