1d3j: Difference between revisions
New page: left|200px<br /><applet load="1d3j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d3j, resolution 1.97Å" /> '''N-TERMINAL DOMAIN CO... |
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[[Image:1d3j.jpg|left|200px]]<br /><applet load="1d3j" size=" | [[Image:1d3j.jpg|left|200px]]<br /><applet load="1d3j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1d3j, resolution 1.97Å" /> | caption="1d3j, resolution 1.97Å" /> | ||
'''N-TERMINAL DOMAIN CORE METHIONINE MUTATION'''<br /> | '''N-TERMINAL DOMAIN CORE METHIONINE MUTATION'''<br /> | ||
==Overview== | ==Overview== | ||
Using heavily methionine-substituted T4 lysozyme as an example, it is | Using heavily methionine-substituted T4 lysozyme as an example, it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large number of singly substituted lysozymes, it is shown that the optimal amino acid to be substituted by methionine is leucine, followed, in order of preference, by phenylalanine, isoleucine and valine. The identification of leucine as the first choice agrees with the ranking suggested by the Dayhoff mutation probability, i.e. by the frequency of amino-acid substitutions in the sequences of related proteins. The ranking of the second and subsequent choices, however, differ significantly. | ||
==About this Structure== | ==About this Structure== | ||
1D3J 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 HED 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:// | 1D3J 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=HED:'>HED</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=1D3J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gassner, N | [[Category: Gassner, N C.]] | ||
[[Category: Matthews, B | [[Category: Matthews, B W.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: HED]] | [[Category: HED]] | ||
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[[Category: t4 lysozyme]] | [[Category: t4 lysozyme]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:34 2008'' | ||
Revision as of 13:12, 21 February 2008
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N-TERMINAL DOMAIN CORE METHIONINE MUTATION
OverviewOverview
Using heavily methionine-substituted T4 lysozyme as an example, it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large number of singly substituted lysozymes, it is shown that the optimal amino acid to be substituted by methionine is leucine, followed, in order of preference, by phenylalanine, isoleucine and valine. The identification of leucine as the first choice agrees with the ranking suggested by the Dayhoff mutation probability, i.e. by the frequency of amino-acid substitutions in the sequences of related proteins. The ranking of the second and subsequent choices, however, differ significantly.
About this StructureAbout this Structure
1D3J 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.
ReferenceReference
Use of differentially substituted selenomethionine proteins in X-ray structure determination., Gassner NC, Matthews BW, Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1967-70. PMID:10666571
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