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PDBsum entry 2qb0
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Hydrolase regulator
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PDB id
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2qb0
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References listed in PDB file
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Key reference
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Title
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Polymer-Driven crystallization.
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Authors
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S.Nauli,
S.Farr,
Y.J.Lee,
H.Y.Kim,
S.Faham,
J.U.Bowie.
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Ref.
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Protein Sci, 2007,
16,
2542-2551.
[DOI no: ]
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PubMed id
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Abstract
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Obtaining well-diffracting crystals of macromolecules remains a significant
barrier to structure determination. Here we propose and test a new approach to
crystallization, in which the crystallization target is fused to a polymerizing
protein module, so that polymer formation drives crystallization of the target.
We test the approach using a polymerization module called 2TEL, which consists
of two tandem sterile alpha motif (SAM) domains from the protein translocation
Ets leukemia (TEL). The 2TEL module is engineered to polymerize as the pH is
lowered, which allows the subtle modulation of polymerization needed for crystal
formation. We show that the 2TEL module can drive the crystallization of 11
soluble proteins, including three that resisted prior crystallization attempts.
In addition, the 2TEL module crystallizes in the presence of various detergents,
suggesting that it might facilitate membrane protein crystallization. The
crystal structures of two fusion proteins show that the TELSAM polymer is
responsible for the majority of contacts in the crystal lattice. The results
suggest that biological polymers could be designed as crystallization modules.
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Figure 4.
Figure 4. Crystal structures and packing of the 2TEL module (sticks model) fused to T4 lysozyme (ribbon diagram) viewed down the
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2007,
16,
2542-2551)
copyright 2007.
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