1sna

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(New page: 200px<br /><applet load="1sna" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sna, resolution 1.50&Aring;" /> '''An Oligomeric Domain...)
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[[Image:1sna.gif|left|200px]]<br /><applet load="1sna" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sna, resolution 1.50&Aring;" />
 
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'''An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein'''<br />
 
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==Overview==
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==An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein==
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The x-ray crystal structure of an oligomeric miniprotein has been, determined to a 1.2-A resolution by means of multiwavelength anomalous, diffraction phasing with selenomethionine analogs that retain the, biophysical characteristics of the native peptide. Peptide 1, comprising, alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously, uncharacterized quaternary structure in which alpha and beta components, interact to form a tightly packed and well defined hydrophobic core. The, structure provides insight into the origins of the unusual thermal, stability of the oligomer. The miniprotein shares many characteristics of, larger proteins, including cooperative folding, lack of, 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.
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<StructureSection load='1sna' size='340' side='right'caption='[[1sna]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sna]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SNA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DBZ:3-(BENZOYLAMINO)-L-ALANINE'>DBZ</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MSO:SELENOMETHIONINE+SELENOXIDE'>MSO</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sna OCA], [https://pdbe.org/1sna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sna RCSB], [https://www.ebi.ac.uk/pdbsum/1sna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sna ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.
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==About this Structure==
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X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture.,Ali MH, Peisach E, Allen KN, Imperiali B Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:15302930<ref>PMID:15302930</ref>
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1SNA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE, NH2 and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SNA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture., Ali MH, Peisach E, Allen KN, Imperiali B, Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15302930 15302930]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1sna" style="background-color:#fffaf0;"></div>
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[[Category: Ali, M.H.]]
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== References ==
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[[Category: Allen, K.N.]]
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<references/>
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[[Category: Imperiali, B.]]
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__TOC__
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[[Category: Peisach, E.]]
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</StructureSection>
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[[Category: ACE]]
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[[Category: Large Structures]]
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[[Category: IPA]]
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[[Category: Ali MH]]
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[[Category: NH2]]
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[[Category: Allen KN]]
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[[Category: domain swapping]]
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[[Category: Imperiali B]]
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[[Category: mini-protein]]
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[[Category: Peisach E]]
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[[Category: oligomerization]]
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[[Category: protein design]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:50:21 2007''
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An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein

PDB ID 1sna

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