1yod

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(New page: 200px<br /><applet load="1yod" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yod, resolution 1.80&Aring;" /> '''Crystal structure of...)
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caption="1yod, resolution 1.80&Aring;" />
caption="1yod, resolution 1.80&Aring;" />
'''Crystal structure of a water soluble analog of phospholamban'''<br />
'''Crystal structure of a water soluble analog of phospholamban'''<br />
==Overview==
==Overview==
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Phospholamban (PLB) is a pentameric transmembrane protein that regulates, the Ca(2+)-dependent ATPase SERCA2a in sarcoplasmic reticulum membranes., We previously described the computational design of a water-soluble, variant of phospholamban, WSPLB, which reproduced many of the structural, and functional properties of the native membrane-soluble protein. While, the full-length WSPLB forms a pentamer in solution, a truncated variant, forms very stable tetramers. To obtain insight into the tetramer-pentamer, cytoplasmic switch, we solved the crystal structure of the truncated, construct, WSPLB 21-52. This peptide has a heptad sequence repeat with Leu, residues at a- and Ile at d-positions from residues 31-52. The crystal, structure revealed that WSPLB 21-52 adopted an antiparallel tetrameric, coiled coil. This topology contrasts with the parallel topology of an, analogue of the coiled-coil of GCN4 with the same Leu(a) Ile(d) repeat., Analysis of these structures revealed how the nature of the partially, exposed residues at e- and g-positions influence the topology formed by, the bundle. We also constructed a model for the pentameric form of PLB, using the coiled-coil parameters derived from a single monomer in the, tetrameric structure. This model suggests that both buried and interfacial, hydrogen bonds are important for stabilizing the parallel pentamer.
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Phospholamban (PLB) is a pentameric transmembrane protein that regulates the Ca(2+)-dependent ATPase SERCA2a in sarcoplasmic reticulum membranes. We previously described the computational design of a water-soluble variant of phospholamban, WSPLB, which reproduced many of the structural and functional properties of the native membrane-soluble protein. While the full-length WSPLB forms a pentamer in solution, a truncated variant forms very stable tetramers. To obtain insight into the tetramer-pentamer cytoplasmic switch, we solved the crystal structure of the truncated construct, WSPLB 21-52. This peptide has a heptad sequence repeat with Leu residues at a- and Ile at d-positions from residues 31-52. The crystal structure revealed that WSPLB 21-52 adopted an antiparallel tetrameric coiled coil. This topology contrasts with the parallel topology of an analogue of the coiled-coil of GCN4 with the same Leu(a) Ile(d) repeat. Analysis of these structures revealed how the nature of the partially exposed residues at e- and g-positions influence the topology formed by the bundle. We also constructed a model for the pentameric form of PLB using the coiled-coil parameters derived from a single monomer in the tetrameric structure. This model suggests that both buried and interfacial hydrogen bonds are important for stabilizing the parallel pentamer.
==About this Structure==
==About this Structure==
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1YOD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YOD OCA].
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1YOD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOD OCA].
==Reference==
==Reference==
X-ray structure of a water-soluble analog of the membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled coils., Slovic AM, Stayrook SE, North B, Degrado WF, J Mol Biol. 2005 May 6;348(3):777-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15826670 15826670]
X-ray structure of a water-soluble analog of the membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled coils., Slovic AM, Stayrook SE, North B, Degrado WF, J Mol Biol. 2005 May 6;348(3):777-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15826670 15826670]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: DeGrado, W.F.]]
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[[Category: DeGrado, W F.]]
[[Category: North, B.]]
[[Category: North, B.]]
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[[Category: Slovic, A.M.]]
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[[Category: Slovic, A M.]]
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[[Category: Stayrook, S.E.]]
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[[Category: Stayrook, S E.]]
[[Category: protein design]]
[[Category: protein design]]
[[Category: water-soluble]]
[[Category: water-soluble]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:26:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:25 2008''

Revision as of 14:07, 21 February 2008


1yod, resolution 1.80Å

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Crystal structure of a water soluble analog of phospholamban

Overview

Phospholamban (PLB) is a pentameric transmembrane protein that regulates the Ca(2+)-dependent ATPase SERCA2a in sarcoplasmic reticulum membranes. We previously described the computational design of a water-soluble variant of phospholamban, WSPLB, which reproduced many of the structural and functional properties of the native membrane-soluble protein. While the full-length WSPLB forms a pentamer in solution, a truncated variant forms very stable tetramers. To obtain insight into the tetramer-pentamer cytoplasmic switch, we solved the crystal structure of the truncated construct, WSPLB 21-52. This peptide has a heptad sequence repeat with Leu residues at a- and Ile at d-positions from residues 31-52. The crystal structure revealed that WSPLB 21-52 adopted an antiparallel tetrameric coiled coil. This topology contrasts with the parallel topology of an analogue of the coiled-coil of GCN4 with the same Leu(a) Ile(d) repeat. Analysis of these structures revealed how the nature of the partially exposed residues at e- and g-positions influence the topology formed by the bundle. We also constructed a model for the pentameric form of PLB using the coiled-coil parameters derived from a single monomer in the tetrameric structure. This model suggests that both buried and interfacial hydrogen bonds are important for stabilizing the parallel pentamer.

About this Structure

1YOD is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

X-ray structure of a water-soluble analog of the membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled coils., Slovic AM, Stayrook SE, North B, Degrado WF, J Mol Biol. 2005 May 6;348(3):777-87. PMID:15826670

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