2zd0

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[[Image:2zd0.jpg|left|200px]]
 
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==Crystal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP)==
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The line below this paragraph, containing "STRUCTURE_2zd0", creates the "Structure Box" on the page.
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<StructureSection load='2zd0' size='340' side='right'caption='[[2zd0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2zd0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZD0 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]] 2.5&#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=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
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{{STRUCTURE_2zd0| PDB=2zd0 | SCENE= }}
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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=2zd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd0 OCA], [https://pdbe.org/2zd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zd0 RCSB], [https://www.ebi.ac.uk/pdbsum/2zd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zd0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTRB_GEOSE MTRB_GEOSE]
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zd/2zd0_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=2zd0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ability of proteins to self-assemble into complex, functional nanoscale structures is expected to become of significant use in the manufacture of artificial nanodevices with a wide range of novel applications. The bacterial protein TRAP has potential uses as a nanoscale component as it is ring-shaped, with a central, modifiable cavity. Furthermore, it can be engineered to make a ring of 12-fold symmetry, which is advantageous for packing into two-dimensional arrays. The 12mer form of TRAP is made by linking multiple subunits together on the same polypeptide, but the usefulness of the 12mers described to date is limited by their poor stability. Here we show that, by altering the length of the peptide linker between subunits, the thermostability can be significantly improved. Since the subunit interfaces of the different 12mers are essentially identical, stabilization arises from the reduction of strain in the linkers. Such a simple method of controlling the stability of modular proteins may have wide applications, and demonstrates the lack of absolute correlation between interactions observable by crystallography and the internal energy of a complex.
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'''Crytal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP)'''
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Intersubunit linker length as a modifier of protein stability: crystal structures and thermostability of mutant TRAP.,Watanabe M, Mishima Y, Yamashita I, Park SY, Tame JR, Heddle JG Protein Sci. 2008 Mar;17(3):518-26. PMID:18287284<ref>PMID:18287284</ref>
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==Overview==
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The ability of proteins to self-assemble into complex, functional nanoscale structures is expected to become of significant use in the manufacture of artificial nanodevices with a wide range of novel applications. The bacterial protein TRAP has potential uses as a nanoscale component as it is ring-shaped, with a central, modifiable cavity. Furthermore, it can be engineered to make a ring of 12-fold symmetry, which is advantageous for packing into two-dimensional arrays. The 12mer form of TRAP is made by linking multiple subunits together on the same polypeptide, but the usefulness of the 12mers described to date is limited by their poor stability. Here we show that, by altering the length of the peptide linker between subunits, the thermostability can be significantly improved. Since the subunit interfaces of the different 12mers are essentially identical, stabilization arises from the reduction of strain in the linkers. Such a simple method of controlling the stability of modular proteins may have wide applications, and demonstrates the lack of absolute correlation between interactions observable by crystallography and the internal energy of a complex.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2ZD0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZD0 OCA].
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</div>
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<div class="pdbe-citations 2zd0" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Intersubunit linker length as a modifier of protein stability: crystal structures and thermostability of mutant TRAP., Watanabe M, Mishima Y, Yamashita I, Park SY, Tame JR, Heddle JG, Protein Sci. 2008 Mar;17(3):518-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18287284 18287284]
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*[[Tryptophan RNA-binding attenuation protein|Tryptophan RNA-binding attenuation protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Heddle, J G.]]
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[[Category: Heddle JG]]
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[[Category: Mishima, Y.]]
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[[Category: Mishima Y]]
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[[Category: Park, S Y.]]
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[[Category: Park SY]]
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[[Category: Tame, J R.H.]]
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[[Category: Tame JRH]]
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[[Category: Watanabe, M.]]
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[[Category: Watanabe M]]
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[[Category: Yamashita, I.]]
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[[Category: Yamashita I]]
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[[Category: 12-mer]]
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[[Category: Artificial]]
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[[Category: Engineered]]
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[[Category: Linker]]
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[[Category: Ring protein]]
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[[Category: Rna binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:31:13 2008''
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Current revision

Crystal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP)

PDB ID 2zd0

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