1mvk
From Proteopedia
(New page: 200px<br /><applet load="1mvk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mvk, resolution 2.5Å" /> '''X-ray structure of th...) |
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| - | [[Image:1mvk.gif|left|200px]]<br /><applet load="1mvk" size=" | + | [[Image:1mvk.gif|left|200px]]<br /><applet load="1mvk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mvk, resolution 2.5Å" /> | caption="1mvk, resolution 2.5Å" /> | ||
'''X-ray structure of the tetrameric mutant of the B1 domain of streptococcal protein G'''<br /> | '''X-ray structure of the tetrameric mutant of the B1 domain of streptococcal protein G'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of a mutant immunoglobulin-binding B1 domain of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1MVK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._group_g Streptococcus sp. group g] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MVK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._group_g Streptococcus sp. group g] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dobrodumov, A.]] | [[Category: Dobrodumov, A.]] | ||
[[Category: Dyda, F.]] | [[Category: Dyda, F.]] | ||
| - | [[Category: Frank, M | + | [[Category: Frank, M K.]] |
| - | [[Category: Gronenborn, A | + | [[Category: Gronenborn, A M.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: channel]] | [[Category: channel]] | ||
[[Category: strand-exchanged tetramer]] | [[Category: strand-exchanged tetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:27 2008'' |
Revision as of 11:59, 21 February 2008
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X-ray structure of the tetrameric mutant of the B1 domain of streptococcal protein G
Overview
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.
About this Structure
1MVK is a Single protein structure of sequence from Streptococcus sp. group g with as ligand. Full crystallographic information is available from OCA.
Reference
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:12379842
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