2qar

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==About this Structure==
==About this Structure==
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2QAR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_tw28 Enterobacteria phage tw28] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=NH4:'>NH4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QAR OCA].
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2QAR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=NH4:'>NH4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Known structural/functional Sites: <scene name='pdbsite=AC1:No3+Binding+Site+For+Residue+D+101'>AC1</scene>, <scene name='pdbsite=AC2:No3+Binding+Site+For+Residue+A+102'>AC2</scene>, <scene name='pdbsite=AC3:No3+Binding+Site+For+Residue+E+108'>AC3</scene>, <scene name='pdbsite=AC4:No3+Binding+Site+For+Residue+D+104'>AC4</scene>, <scene name='pdbsite=AC5:No3+Binding+Site+For+Residue+D+106'>AC5</scene>, <scene name='pdbsite=AC6:No3+Binding+Site+For+Residue+E+109'>AC6</scene>, <scene name='pdbsite=AC7:No3+Binding+Site+For+Residue+D+108'>AC7</scene>, <scene name='pdbsite=AC8:No3+Binding+Site+For+Residue+B+109'>AC8</scene>, <scene name='pdbsite=AC9:Nh4+Binding+Site+For+Residue+A+201'>AC9</scene> and <scene name='pdbsite=BC1:Nh4+Binding+Site+For+Residue+D+202'>BC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QAR OCA].
==Reference==
==Reference==
Polymer-driven crystallization., Nauli S, Farr S, Lee YJ, Kim HY, Faham S, Bowie JU, Protein Sci. 2007 Nov;16(11):2542-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17962407 17962407]
Polymer-driven crystallization., Nauli S, Farr S, Lee YJ, Kim HY, Faham S, Bowie JU, Protein Sci. 2007 Nov;16(11):2542-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17962407 17962407]
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[[Category: Enterobacteria phage tw28]]
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[[Category: Bacteriophage t4]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: sterile alpha motif]]
[[Category: sterile alpha motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 15:31:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:28:46 2008''

Revision as of 15:28, 6 February 2008


2qar, resolution 2.400Å

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Structure of the 2TEL crystallization module fused to T4 lysozyme with a helical linker.

Overview

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.

About this Structure

2QAR is a Protein complex structure of sequences from Bacteriophage t4 and Escherichia coli with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , , , , , , , , and . Full crystallographic information is available from OCA.

Reference

Polymer-driven crystallization., Nauli S, Farr S, Lee YJ, Kim HY, Faham S, Bowie JU, Protein Sci. 2007 Nov;16(11):2542-51. PMID:17962407

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