1sap: Difference between revisions

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[[Image:1sap.gif|left|200px]]
{{Seed}}
[[Image:1sap.png|left|200px]]


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{{STRUCTURE_1sap|  PDB=1sap  |  SCENE=  }}  
{{STRUCTURE_1sap|  PDB=1sap  |  SCENE=  }}  


'''HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE'''
===HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7577913}}


==About this Structure==
==About this Structure==
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].  
1SAP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAP OCA].  


==Reference==
==Reference==
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[[Category: Shriver, J W.]]
[[Category: Shriver, J W.]]
[[Category: Dna-binding protein]]
[[Category: Dna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:05:13 2008''

Revision as of 01:05, 28 July 2008

File:1sap.png

Template:STRUCTURE 1sap

HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE

Template:ABSTRACT PUBMED 7577913

About this Structure

1SAP is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full experimental 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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