2tsa: Difference between revisions
New page: left|200px<br /><applet load="2tsa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2tsa, resolution 2.2Å" /> '''AZURIN MUTANT M121A''... |
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[[Image:2tsa.jpg|left|200px]]<br /><applet load="2tsa" size=" | [[Image:2tsa.jpg|left|200px]]<br /><applet load="2tsa" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2tsa, resolution 2.2Å" /> | caption="2tsa, resolution 2.2Å" /> | ||
'''AZURIN MUTANT M121A'''<br /> | '''AZURIN MUTANT M121A'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structures of the azurin mutant Met121Ala and its azide | The crystal structures of the azurin mutant Met121Ala and its azide derivative Met121Ala-azide from Pseudomonas aeruginosa have been determined. The final crystallographic R values are 21.3 and 19.4% for the two structures, respectively. In the Met121Ala mutant, the distance between the copper ion and His117 increases by 0.34 A compared with the wild-type structure. The removal of the methionine in the apical position induces a shortening of the distance from the copper ion to the carbonyl O atom of Gly45 from 2.97 to 2.74 A. In the Met121Ala-azide structure, the azide anion occupies the cavity created by replacing the Met121 side chain with the smaller methyl group of Ala. The azide anion binds with a terminal N atom to the copper ion at a distance of about 2.04 A. In addition, the copper ion has moved out of the trigonal plane by about 0.26 A towards the azide anion. Thus, the copper site in this structure has a distorted tetrahedral arrangement. The spectroscopic characteristics show, in addition, that the copper sites in the two structures are distinctively different. The Met121Ala mutant still maintains the properties of an ordinary type 1 copper site while the Met121Ala-azide derivative has an absorption maximum at about 409 nm and the copper hyperfine coupling has increased to a value intermediate between those of type 2 copper and the wild-type azurin. | ||
==About this Structure== | ==About this Structure== | ||
2TSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | 2TSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1TSA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TSA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bonander, N.]] | [[Category: Bonander, N.]] | ||
[[Category: Harata, K.]] | [[Category: Harata, K.]] | ||
[[Category: Karlsson, B | [[Category: Karlsson, B G.]] | ||
[[Category: Langer, V.]] | [[Category: Langer, V.]] | ||
[[Category: Sjolin, L.]] | [[Category: Sjolin, L.]] | ||
[[Category: Tsai, L | [[Category: Tsai, L C.]] | ||
[[Category: Vanngard, T.]] | [[Category: Vanngard, T.]] | ||
[[Category: CU]] | [[Category: CU]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
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Revision as of 19:50, 21 February 2008
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AZURIN MUTANT M121A
OverviewOverview
The crystal structures of the azurin mutant Met121Ala and its azide derivative Met121Ala-azide from Pseudomonas aeruginosa have been determined. The final crystallographic R values are 21.3 and 19.4% for the two structures, respectively. In the Met121Ala mutant, the distance between the copper ion and His117 increases by 0.34 A compared with the wild-type structure. The removal of the methionine in the apical position induces a shortening of the distance from the copper ion to the carbonyl O atom of Gly45 from 2.97 to 2.74 A. In the Met121Ala-azide structure, the azide anion occupies the cavity created by replacing the Met121 side chain with the smaller methyl group of Ala. The azide anion binds with a terminal N atom to the copper ion at a distance of about 2.04 A. In addition, the copper ion has moved out of the trigonal plane by about 0.26 A towards the azide anion. Thus, the copper site in this structure has a distorted tetrahedral arrangement. The spectroscopic characteristics show, in addition, that the copper sites in the two structures are distinctively different. The Met121Ala mutant still maintains the properties of an ordinary type 1 copper site while the Met121Ala-azide derivative has an absorption maximum at about 409 nm and the copper hyperfine coupling has increased to a value intermediate between those of type 2 copper and the wild-type azurin.
About this StructureAbout this Structure
2TSA is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. This structure supersedes the now removed PDB entry 1TSA. Full crystallographic information is available from OCA.
ReferenceReference
Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structures and spectral properties., Tsai LC, Bonander N, Harata K, Karlsson G, Vanngard T, Langer V, Sjolin L, Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):950-8. PMID:15299604
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