1sn9

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(New page: 200px<br /><applet load="1sn9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sn9, resolution 1.20&Aring;" /> '''An Oligomeric Domain...)
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[[Image:1sn9.gif|left|200px]]<br /><applet load="1sn9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sn9, resolution 1.20&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='1sn9' size='340' side='right'caption='[[1sn9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sn9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SN9 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]] 1.2&#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=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=1sn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sn9 OCA], [https://pdbe.org/1sn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sn9 RCSB], [https://www.ebi.ac.uk/pdbsum/1sn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sn9 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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1SN9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SN9 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 1sn9" 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: NH2]]
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[[Category: Ali MH]]
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[[Category: domain swapping]]
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[[Category: Allen KN]]
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[[Category: mini-protein]]
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[[Category: Imperiali B]]
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[[Category: oligomerization]]
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[[Category: Peisach E]]
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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 00:50:03 2007''
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Current revision

An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein

PDB ID 1sn9

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