2plh
From Proteopedia
(New page: 200px<br /><applet load="2plh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2plh, resolution 2.5Å" /> '''STRUCTURE OF ALPHA-1-...) |
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| - | [[Image:2plh.jpg|left|200px]]<br /><applet load="2plh" size=" | + | [[Image:2plh.jpg|left|200px]]<br /><applet load="2plh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2plh, resolution 2.5Å" /> | caption="2plh, resolution 2.5Å" /> | ||
'''STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of alpha(1)-purothionin (alpha(1)-PT), a | + | The three-dimensional structure of alpha(1)-purothionin (alpha(1)-PT), a wheat-germ protein and a basic lytic toxin, was previously solved by molecular-replacement methods using an energy-minimized predicted model and refined to an R-factor of 21.6% [Teeter, Ma, Rao & Whitlow (1990). Proteins Struct. Funct. Genet. 8, 118-1321. Some deficiencies of the model motivated us to revisit the structure and to continue the refinement. Here we report a significantly improved structure refined to an R-factor of 15.5% with excellent geometry. The refinement of this relatively low resolution structure ( approximately 2.8 A) is well suited to test the limitations of classical methods of refinement and to address the problem of overfitting, The final structure contains 434 atoms including 330 protein atoms, 70 waters, three acetates, two glycerols, one sec-butanol and one phosphate. The key solute molecules (acetate ion and phosphate ion) play a crucial role in the lattice formation. Phosphate and glycerol found in the structure may be important for biological activity of the toxins. |
==About this Structure== | ==About this Structure== | ||
| - | 2PLH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with ACT, PO4, SBT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2PLH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=SBT:'>SBT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rao, U.]] | [[Category: Rao, U.]] | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
| - | [[Category: Teeter, M | + | [[Category: Teeter, M M.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: membrane active]] | [[Category: membrane active]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:42 2008'' |
Revision as of 16:30, 21 February 2008
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STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of alpha(1)-purothionin (alpha(1)-PT), a wheat-germ protein and a basic lytic toxin, was previously solved by molecular-replacement methods using an energy-minimized predicted model and refined to an R-factor of 21.6% [Teeter, Ma, Rao & Whitlow (1990). Proteins Struct. Funct. Genet. 8, 118-1321. Some deficiencies of the model motivated us to revisit the structure and to continue the refinement. Here we report a significantly improved structure refined to an R-factor of 15.5% with excellent geometry. The refinement of this relatively low resolution structure ( approximately 2.8 A) is well suited to test the limitations of classical methods of refinement and to address the problem of overfitting, The final structure contains 434 atoms including 330 protein atoms, 70 waters, three acetates, two glycerols, one sec-butanol and one phosphate. The key solute molecules (acetate ion and phosphate ion) play a crucial role in the lattice formation. Phosphate and glycerol found in the structure may be important for biological activity of the toxins.
About this Structure
2PLH is a Single protein structure of sequence from Triticum aestivum with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 1: alpha1-purothionin revisited., Rao U, Stec B, Teeter MM, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):904-13. PMID:15299760
Page seeded by OCA on Thu Feb 21 18:30:42 2008
Categories: Single protein | Triticum aestivum | Rao, U. | Stec, B. | Teeter, M M. | ACT | GOL | PO4 | SBT | Disulfide rich | Membrane active
