1nay

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[[Image:1nay.gif|left|200px]]
 
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{{Structure
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==GPP-Foldon:X-ray structure==
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|PDB= 1nay |SIZE=350|CAPTION= <scene name='initialview01'>1nay</scene>, resolution 2.60&Aring;
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<StructureSection load='1nay' size='340' side='right'caption='[[1nay]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1nay]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NAY FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=1nay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nay OCA], [https://pdbe.org/1nay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nay RCSB], [https://www.ebi.ac.uk/pdbsum/1nay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nay ProSAT]</span></td></tr>
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}}
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</table>
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== Evolutionary Conservation ==
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'''GPP-Foldon:X-ray structure'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/na/1nay_consurf.spt"</scriptWhenChecked>
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In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1NAY is a [[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=1NAY OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nay ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon., Stetefeld J, Frank S, Jenny M, Schulthess T, Kammerer RA, Boudko S, Landwehr R, Okuyama K, Engel J, Structure. 2003 Mar;11(3):339-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12623021 12623021]
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</StructureSection>
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[[Category: Protein complex]]
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[[Category: Escherichia coli]]
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[[Category: Stetefeld, J.]]
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[[Category: Large Structures]]
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[[Category: collagen assembly]]
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[[Category: Stetefeld J]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:25 2008''
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Current revision

GPP-Foldon:X-ray structure

PDB ID 1nay

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