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PDBsum entry 1d3f
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Use of differentially substituted selenomethionine proteins in X-Ray structure determination.
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Authors
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N.C.Gassner,
B.W.Matthews.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
1967-1970.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Methionine and alanine substitutions show that the formation of wild-Type-Like structure in the carboxy-Terminal domain of t4 lysozyme is a rate-Limiting step in folding.
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Authors
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N.C.Gassner,
W.A.Baase,
J.D.Lindstrom,
J.Lu,
F.W.Dahlquist,
B.W.Matthews.
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Ref.
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Biochemistry, 1999,
38,
14451-14460.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of t4 lysozyme.
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Authors
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N.C.Gassner,
W.A.Baase,
B.W.Matthews.
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Ref.
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Proc Natl Acad Sci U S A, 1996,
93,
12155-12158.
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PubMed id
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Secondary reference #3
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Title
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Structure of bacteriophage t4 lysozyme refined at 1.7 a resolution.
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Authors
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L.H.Weaver,
B.W.Matthews.
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Ref.
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J Mol Biol, 1987,
193,
189-199.
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PubMed id
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