1nqm

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[[Image:1nqm.gif|left|200px]]
 
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==Structure of Savm-W120K, streptavidin mutant==
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The line below this paragraph, containing "STRUCTURE_1nqm", creates the "Structure Box" on the page.
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<StructureSection load='1nqm' size='340' side='right'caption='[[1nqm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1nqm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NQM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.7&#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=BTN:BIOTIN'>BTN</scene></td></tr>
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{{STRUCTURE_1nqm| PDB=1nqm | 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=1nqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqm OCA], [https://pdbe.org/1nqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nqm RCSB], [https://www.ebi.ac.uk/pdbsum/1nqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nqm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
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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/nq/1nqm_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=1nqm ConSurf].
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<div style="clear:both"></div>
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'''Structure of Savm-W120K, streptavidin mutant'''
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==See Also==
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*[[Avidin 3D structures|Avidin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The biotin-binding tetrameric proteins, streptavidin from Streptomyces avidinii and chicken egg white avidin, are excellent models for the study of subunit-subunit interactions of a multimeric protein. Efforts are thus being made to prepare mutated forms of streptavidin and avidin, which would form monomers or dimers, in order to examine their effect on quaternary structure and assembly. In the present communication, we compared the crystal structures of binding site W--&gt;K mutations in streptavidin and avidin. In solution, both mutant proteins are known to form dimers, but upon crystallization, both formed tetramers with the same parameters as the native proteins. All of the intersubunit bonds were conserved, except for the hydrophobic interaction between biotin and the tryptophan that was replaced by lysine. In the crystal structure, the binding site of the mutated apo-avidin contains 3 molecules of structured water instead of the 5 contained in the native protein. The lysine side chain extends in a direction opposite that of the native tryptophan, the void being partially filled by an adjacent lysine residue. Nevertheless, the binding-site conformation observed for the mutant tetramer is an artificial consequence of crystal packing that would not be maintained in the solution-phase dimer. It appears that the dimer-tetramer transition may be concentration dependent, and the interaction among subunits obeys the law of mass action.
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[[Category: Large Structures]]
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==About this Structure==
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1NQM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQM OCA].
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==Reference==
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Dimer-tetramer transition between solution and crystalline states of streptavidin and avidin mutants., Pazy Y, Eisenberg-Domovich Y, Laitinen OH, Kulomaa MS, Bayer EA, Wilchek M, Livnah O, J Bacteriol. 2003 Jul;185(14):4050-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837778 12837778]
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[[Category: Single protein]]
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[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
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[[Category: Bayer, E A.]]
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[[Category: Bayer EA]]
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[[Category: Eisenberg-Domovich, Y.]]
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[[Category: Eisenberg-Domovich Y]]
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[[Category: Kulomaa, M S.]]
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[[Category: Kulomaa MS]]
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[[Category: Laitinen, O H.]]
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[[Category: Laitinen OH]]
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[[Category: Livnah, O.]]
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[[Category: Livnah O]]
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[[Category: Pazy, Y.]]
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[[Category: Pazy Y]]
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[[Category: Wilchek, M.]]
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[[Category: Wilchek M]]
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[[Category: Avidin]]
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[[Category: Biotin]]
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[[Category: High affinity system]]
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[[Category: Monomer-monomer interaction]]
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[[Category: Streptavidin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:51:51 2008''
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Current revision

Structure of Savm-W120K, streptavidin mutant

PDB ID 1nqm

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