1mvk

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[[Image:1mvk.gif|left|200px]]
 
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{{Structure
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==X-ray structure of the tetrameric mutant of the B1 domain of streptococcal protein G==
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|PDB= 1mvk |SIZE=350|CAPTION= <scene name='initialview01'>1mvk</scene>, resolution 2.5&Aring;
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<StructureSection load='1mvk' size='340' side='right'caption='[[1mvk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1mvk]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVK 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]] 2.5&#8491;</td></tr>
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|GENE= SPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1mvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvk OCA], [https://pdbe.org/1mvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvk RCSB], [https://www.ebi.ac.uk/pdbsum/1mvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvk ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1mpe|1MPE]], [[1gb1|1GB1]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvk OCA], [http://www.ebi.ac.uk/pdbsum/1mvk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mvk RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
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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/mv/1mvk_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=1mvk ConSurf].
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<div style="clear:both"></div>
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'''X-ray structure of the tetrameric mutant of the B1 domain of streptococcal protein G'''
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==See Also==
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*[[Protein G|Protein G]]
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__TOC__
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==Overview==
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</StructureSection>
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The structure of a mutant immunoglobulin-binding B1 domain of streptococcal protein G (GB1), which comprises five conservative changes in hydrophobic core residues, was determined by NMR spectroscopy and X-ray crystallography. The oligomeric state and quaternary structure of the mutant protein are drastically changed from the wild type protein. The mutant structure consists of a symmetric tetramer, with intermolecular strand exchange involving all four units. Four of the five secondary structure elements present in the monomeric wild type GB1 structure are retained in the tetrameric structure, although their intra- and intermolecular interactions are altered. Our results demonstrate that through the acquisition of a moderate number of pivotal point mutations, proteins such as GB1 are able to undergo drastic structural changes, overcoming reduced stability of the monomeric unit by multimerization. The present structure is an illustrative example of how proteins exploit the breadth of conformational space.
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[[Category: Large Structures]]
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[[Category: Streptococcus sp. 'group G']]
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==About this Structure==
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[[Category: Dobrodumov A]]
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1MVK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVK OCA].
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[[Category: Dyda F]]
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[[Category: Frank MK]]
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==Reference==
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[[Category: Gronenborn AM]]
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Core mutations switch monomeric protein GB1 into an intertwined tetramer., Kirsten Frank M, Dyda F, Dobrodumov A, Gronenborn AM, Nat Struct Biol. 2002 Nov;9(11):877-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12379842 12379842]
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[[Category: Bacteria]]
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[[Category: Single protein]]
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[[Category: Dobrodumov, A.]]
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[[Category: Dyda, F.]]
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[[Category: Frank, M K.]]
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[[Category: Gronenborn, A M.]]
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[[Category: channel]]
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[[Category: strand-exchanged tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:50 2008''
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Current revision

X-ray structure of the tetrameric mutant of the B1 domain of streptococcal protein G

PDB ID 1mvk

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