1yhb

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(New page: 200px<br /><applet load="1yhb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yhb, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURES OF...)
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'''CRYSTAL STRUCTURES OF Y41H AND Y41F MUTANTS OF GENE V PROTEIN FROM FF PHAGE SUGGEST POSSIBLE PROTEIN-PROTEIN INTERACTIONS IN GVP-SSDNA COMPLEX'''<br />
'''CRYSTAL STRUCTURES OF Y41H AND Y41F MUTANTS OF GENE V PROTEIN FROM FF PHAGE SUGGEST POSSIBLE PROTEIN-PROTEIN INTERACTIONS IN GVP-SSDNA COMPLEX'''<br />
==Overview==
==Overview==
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Gene V protein (GVP) encoded by the filamentous phage Ff (M13, fl, fd) is, a homodimeric protein of 87 amino acids that binds to single-stranded DNA, (ssDNA) nonspecifically and cooperatively. The structure (monoclinic C2, form) of the wild-type protein has been determined and refined at 1.8-A, resolution [Skinner et al. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2071-2075]. The monomer structure consists of a somewhat distorted, five-stranded beta-barrel core with three prominent loops: a DNA-binding, loop, a dyad loop, and a dimer contact loop. The amino acid residue at, position 41 plays an important role in the dimer-dimer interactions of the, protein-ssDNA complex. Two Y41 mutant structures have been studied by, X-ray crystallography. The Y41F GVP structure has been refined to an, R-factor of 0.180 at 2.2-A resolution and is very similar to the wild-type, (wt) structure (rmsd of all C alpha atoms = 0.30 A). In contrast, Y41H GVP, forms a new crystal lattice in the space group P2(1)2(1)2(1) with a =, 77.18 A, b = 84.17 A, and c = 28.62 A. Its structure has been solved by, the molecular replacement method and refined to an R-factor of 0.170 at, 2.5-A resolution. The two monomers of Y41H are crystallographically, independent, and their structures remain similar to wt-GVP but with, significant differences, particularly in the DNA-binding hairpin region., In both crystals, the loop (residues 36-43) that contains the Y41 residue, is involved in the crystal dimer packings but in a different manner. The, dimer-dimer contacts found in the wt-GVP crystal may be important for GVP, aggregation in the absence of DNA. In the presence of DNA, the dimer-dimer, contacts may switch to the type found in the Y41H crystal, allowing the, GVP-ssDNA complex to form cooperatively. A model of the complex, consistent with existing biochemical and biophysical data, has been, constructed from those crystal packing data.
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Gene V protein (GVP) encoded by the filamentous phage Ff (M13, fl, fd) is a homodimeric protein of 87 amino acids that binds to single-stranded DNA (ssDNA) nonspecifically and cooperatively. The structure (monoclinic C2 form) of the wild-type protein has been determined and refined at 1.8-A resolution [Skinner et al. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2071-2075]. The monomer structure consists of a somewhat distorted five-stranded beta-barrel core with three prominent loops: a DNA-binding loop, a dyad loop, and a dimer contact loop. The amino acid residue at position 41 plays an important role in the dimer-dimer interactions of the protein-ssDNA complex. Two Y41 mutant structures have been studied by X-ray crystallography. The Y41F GVP structure has been refined to an R-factor of 0.180 at 2.2-A resolution and is very similar to the wild-type (wt) structure (rmsd of all C alpha atoms = 0.30 A). In contrast, Y41H GVP forms a new crystal lattice in the space group P2(1)2(1)2(1) with a = 77.18 A, b = 84.17 A, and c = 28.62 A. Its structure has been solved by the molecular replacement method and refined to an R-factor of 0.170 at 2.5-A resolution. The two monomers of Y41H are crystallographically independent, and their structures remain similar to wt-GVP but with significant differences, particularly in the DNA-binding hairpin region. In both crystals, the loop (residues 36-43) that contains the Y41 residue is involved in the crystal dimer packings but in a different manner. The dimer-dimer contacts found in the wt-GVP crystal may be important for GVP aggregation in the absence of DNA. In the presence of DNA, the dimer-dimer contacts may switch to the type found in the Y41H crystal, allowing the GVP-ssDNA complex to form cooperatively. A model of the complex, consistent with existing biochemical and biophysical data, has been constructed from those crystal packing data.
==About this Structure==
==About this Structure==
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1YHB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_f1 Bacteriophage f1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YHB OCA].
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1YHB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_f1 Bacteriophage f1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YHB OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Guan, Y.]]
[[Category: Guan, Y.]]
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[[Category: Hilbers, C.W.]]
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[[Category: Hilbers, C W.]]
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[[Category: Konings, R.N.H.]]
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[[Category: Konings, R N.H.]]
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[[Category: Terwilliger, T.C.]]
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[[Category: Terwilliger, T C.]]
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[[Category: Wang, A.H.J.]]
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[[Category: Wang, A H.J.]]
[[Category: Zhang, H.]]
[[Category: Zhang, H.]]
[[Category: dna-binding protein]]
[[Category: dna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:17 2008''

Revision as of 14:05, 21 February 2008


1yhb, resolution 2.2Å

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CRYSTAL STRUCTURES OF Y41H AND Y41F MUTANTS OF GENE V PROTEIN FROM FF PHAGE SUGGEST POSSIBLE PROTEIN-PROTEIN INTERACTIONS IN GVP-SSDNA COMPLEX

Overview

Gene V protein (GVP) encoded by the filamentous phage Ff (M13, fl, fd) is a homodimeric protein of 87 amino acids that binds to single-stranded DNA (ssDNA) nonspecifically and cooperatively. The structure (monoclinic C2 form) of the wild-type protein has been determined and refined at 1.8-A resolution [Skinner et al. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2071-2075]. The monomer structure consists of a somewhat distorted five-stranded beta-barrel core with three prominent loops: a DNA-binding loop, a dyad loop, and a dimer contact loop. The amino acid residue at position 41 plays an important role in the dimer-dimer interactions of the protein-ssDNA complex. Two Y41 mutant structures have been studied by X-ray crystallography. The Y41F GVP structure has been refined to an R-factor of 0.180 at 2.2-A resolution and is very similar to the wild-type (wt) structure (rmsd of all C alpha atoms = 0.30 A). In contrast, Y41H GVP forms a new crystal lattice in the space group P2(1)2(1)2(1) with a = 77.18 A, b = 84.17 A, and c = 28.62 A. Its structure has been solved by the molecular replacement method and refined to an R-factor of 0.170 at 2.5-A resolution. The two monomers of Y41H are crystallographically independent, and their structures remain similar to wt-GVP but with significant differences, particularly in the DNA-binding hairpin region. In both crystals, the loop (residues 36-43) that contains the Y41 residue is involved in the crystal dimer packings but in a different manner. The dimer-dimer contacts found in the wt-GVP crystal may be important for GVP aggregation in the absence of DNA. In the presence of DNA, the dimer-dimer contacts may switch to the type found in the Y41H crystal, allowing the GVP-ssDNA complex to form cooperatively. A model of the complex, consistent with existing biochemical and biophysical data, has been constructed from those crystal packing data.

About this Structure

1YHB is a Single protein structure of sequence from Bacteriophage f1. Full crystallographic information is available from OCA.

Reference

Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex., Guan Y, Zhang H, Konings RN, Hilbers CW, Terwilliger TC, Wang AH, Biochemistry. 1994 Jun 28;33(25):7768-78. PMID:8011642

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