1sap
From Proteopedia
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| - | [[Image:1sap.gif|left|200px]] | + | [[Image:1sap.gif|left|200px]] |
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| - | '''HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE''' | + | {{Structure |
| + | |PDB= 1sap |SIZE=350|CAPTION= <scene name='initialview01'>1sap</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SAP is a [ | + | 1SAP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAP OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius., Edmondson SP, Qiu L, Shriver JW, Biochemistry. 1995 Oct 17;34(41):13289-304. PMID:[http:// | + | Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius., Edmondson SP, Qiu L, Shriver JW, Biochemistry. 1995 Oct 17;34(41):13289-304. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7577913 7577913] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus acidocaldarius]] | [[Category: Sulfolobus acidocaldarius]] | ||
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[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:02:29 2008'' |
Revision as of 12:02, 20 March 2008
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HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE
Overview
The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding.
About this Structure
1SAP is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
Reference
Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius., Edmondson SP, Qiu L, Shriver JW, Biochemistry. 1995 Oct 17;34(41):13289-304. PMID:7577913
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