1t6h

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(New page: 200px<br /><applet load="1t6h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6h, resolution 2.01&Aring;" /> '''Crystal Structure T4...)
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[[Image:1t6h.jpg|left|200px]]<br /><applet load="1t6h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t6h, resolution 2.01&Aring;" />
caption="1t6h, resolution 2.01&Aring;" />
'''Crystal Structure T4 Lysozyme incorporating an unnatural amino acid p-iodo-L-phenylalanine at position 153'''<br />
'''Crystal Structure T4 Lysozyme incorporating an unnatural amino acid p-iodo-L-phenylalanine at position 153'''<br />
==Overview==
==Overview==
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A recently developed method makes it possible to genetically encode, unnatural amino acids with diverse physical, chemical or biological, properties in Escherichia coli and yeast. We now show that this technology, can be used to efficiently and site-specifically incorporate, p-iodo-L-phenylalanine (iodoPhe) into proteins in response to an amber TAG, codon. The selective introduction of the anomalously scattering iodine, atom into proteins should facilitate single-wavelength anomalous, dispersion experiments on in-house X-ray sources. To illustrate this, we, generated a Phe153 --&gt; iodoPhe mutant of bacteriophage T4 lysozyme and, determined its crystal structure using considerably less data than are, needed for the equivalent experiment with cysteine and methionine. The, iodoPhe residue, although present in the hydrophobic core of the protein, did not perturb the protein structure in any meaningful way. The ability, to selectively introduce this and other heavy atom-containing amino acids, into proteins should facilitate the structural study of proteins.
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A recently developed method makes it possible to genetically encode unnatural amino acids with diverse physical, chemical or biological properties in Escherichia coli and yeast. We now show that this technology can be used to efficiently and site-specifically incorporate p-iodo-L-phenylalanine (iodoPhe) into proteins in response to an amber TAG codon. The selective introduction of the anomalously scattering iodine atom into proteins should facilitate single-wavelength anomalous dispersion experiments on in-house X-ray sources. To illustrate this, we generated a Phe153 --&gt; iodoPhe mutant of bacteriophage T4 lysozyme and determined its crystal structure using considerably less data than are needed for the equivalent experiment with cysteine and methionine. The iodoPhe residue, although present in the hydrophobic core of the protein, did not perturb the protein structure in any meaningful way. The ability to selectively introduce this and other heavy atom-containing amino acids into proteins should facilitate the structural study of proteins.
==About this Structure==
==About this Structure==
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1T6H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CL and BME 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T6H OCA].
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1T6H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=BME:'>BME</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=1T6H OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brock, A.]]
[[Category: Brock, A.]]
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[[Category: Schultz, P.G.]]
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[[Category: Schultz, P G.]]
[[Category: Spraggon, G.]]
[[Category: Spraggon, G.]]
[[Category: Wang, L.]]
[[Category: Wang, L.]]
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[[Category: unnatural amino acid]]
[[Category: unnatural amino acid]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:01:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:22 2008''

Revision as of 13:10, 21 February 2008


1t6h, resolution 2.01Å

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Crystal Structure T4 Lysozyme incorporating an unnatural amino acid p-iodo-L-phenylalanine at position 153

Overview

A recently developed method makes it possible to genetically encode unnatural amino acids with diverse physical, chemical or biological properties in Escherichia coli and yeast. We now show that this technology can be used to efficiently and site-specifically incorporate p-iodo-L-phenylalanine (iodoPhe) into proteins in response to an amber TAG codon. The selective introduction of the anomalously scattering iodine atom into proteins should facilitate single-wavelength anomalous dispersion experiments on in-house X-ray sources. To illustrate this, we generated a Phe153 --> iodoPhe mutant of bacteriophage T4 lysozyme and determined its crystal structure using considerably less data than are needed for the equivalent experiment with cysteine and methionine. The iodoPhe residue, although present in the hydrophobic core of the protein, did not perturb the protein structure in any meaningful way. The ability to selectively introduce this and other heavy atom-containing amino acids into proteins should facilitate the structural study of proteins.

About this Structure

1T6H is a Single protein structure of sequence from Bacteriophage t4 with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

The site-specific incorporation of p-iodo-L-phenylalanine into proteins for structure determination., Xie J, Wang L, Wu N, Brock A, Spraggon G, Schultz PG, Nat Biotechnol. 2004 Oct;22(10):1297-301. Epub 2004 Sep 19. PMID:15378068

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