1hz5
From Proteopedia
(New page: 200px<br /><applet load="1hz5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hz5, resolution 1.80Å" /> '''CRYSTAL STRUCTURES O...) |
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| - | [[Image:1hz5.jpg|left|200px]]<br /><applet load="1hz5" size=" | + | [[Image:1hz5.jpg|left|200px]]<br /><applet load="1hz5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hz5, resolution 1.80Å" /> | caption="1hz5, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS, WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION'''<br /> | '''CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS, WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a tryptophan-containing variant of the | + | The three-dimensional structure of a tryptophan-containing variant of the IgG-binding B1 domain of protein L has been solved in two crystal forms to 1.7 and 1.8 A resolution. In one of the crystal forms, the entire N-terminal histidine-tag region was immobilized through the coordination of zinc ions and its structural conformation along with the zinc coordination scheme were determined. However, the ordering of the histidine tag by zinc does not affect the overall structure of the rest of the protein. Structural comparisons of the tryptophan-containing variant with an NMR-derived wild-type structure, which contains a tyrosine at position 47, reveals a common fold, although the overall backbone root-mean-square difference is 1.5 A. The Y47W substitution only caused local rearrangement of several side chains, the most prominent of which is the rotation of the Tyr34 side chain, resulting in a 6 A displacement of its hydroxyl group. A small methyl-sized cavity bounded by beta-strands 1, 2 and 4 and the alpha-helix was found in the structures of the Y47W-substituted protein L B1 domain. This cavity may be created as the result of subsequent side-chain rearrangements caused by the Y47W substitution. These high-resolution structures of the tryptophan-containing variant provide a reference frame for the analysis of thermodynamic and kinetic data derived from a series of mutational studies of the protein L B1 domain. |
==About this Structure== | ==About this Structure== | ||
| - | 1HZ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HZ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baker, D.]] | [[Category: Baker, D.]] | ||
| - | [[Category: Kim, D | + | [[Category: Kim, D E.]] |
| - | [[Category: Neill, J | + | [[Category: Neill, J W.O.]] |
| - | [[Category: Zhang, K | + | [[Category: Zhang, K Y.J.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: binds kappa light chain of immunoglobulins]] | [[Category: binds kappa light chain of immunoglobulins]] | ||
| Line 22: | Line 22: | ||
[[Category: zinc coordinated histag]] | [[Category: zinc coordinated histag]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:19 2008'' |
Revision as of 11:06, 21 February 2008
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CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS, WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION
Overview
The three-dimensional structure of a tryptophan-containing variant of the IgG-binding B1 domain of protein L has been solved in two crystal forms to 1.7 and 1.8 A resolution. In one of the crystal forms, the entire N-terminal histidine-tag region was immobilized through the coordination of zinc ions and its structural conformation along with the zinc coordination scheme were determined. However, the ordering of the histidine tag by zinc does not affect the overall structure of the rest of the protein. Structural comparisons of the tryptophan-containing variant with an NMR-derived wild-type structure, which contains a tyrosine at position 47, reveals a common fold, although the overall backbone root-mean-square difference is 1.5 A. The Y47W substitution only caused local rearrangement of several side chains, the most prominent of which is the rotation of the Tyr34 side chain, resulting in a 6 A displacement of its hydroxyl group. A small methyl-sized cavity bounded by beta-strands 1, 2 and 4 and the alpha-helix was found in the structures of the Y47W-substituted protein L B1 domain. This cavity may be created as the result of subsequent side-chain rearrangements caused by the Y47W substitution. These high-resolution structures of the tryptophan-containing variant provide a reference frame for the analysis of thermodynamic and kinetic data derived from a series of mutational studies of the protein L B1 domain.
About this Structure
1HZ5 is a Single protein structure of sequence from Finegoldia magna with as ligand. Full crystallographic information is available from OCA.
Reference
Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution., O'Neill JW, Kim DE, Baker D, Zhang KY, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):480-7. PMID:11264576
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