1mpe
From Proteopedia
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- | [[Image:1mpe.jpg|left|200px]] | + | [[Image:1mpe.jpg|left|200px]] |
- | + | ||
- | '''Ensemble of 20 structures of the tetrameric mutant of the B1 domain of streptococcal protein G''' | + | {{Structure |
+ | |PDB= 1mpe |SIZE=350|CAPTION= <scene name='initialview01'>1mpe</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= SPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Streptococcus sp. group G]) | ||
+ | }} | ||
+ | |||
+ | '''Ensemble of 20 structures of the tetrameric mutant of the B1 domain of streptococcal protein G''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1MPE is a [ | + | 1MPE is a [[Single protein]] structure of sequence from [http://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=1MPE OCA]. |
==Reference== | ==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:[http:// | + | 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] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus sp. group g]] | [[Category: Streptococcus sp. group g]] | ||
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[[Category: strand-exchanged tetramer]] | [[Category: strand-exchanged tetramer]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:27 2008'' |
Revision as of 10:46, 20 March 2008
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Gene: | SPG (Streptococcus sp. group G) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Ensemble of 20 structures 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
1MPE is a Single protein structure of sequence from Streptococcus sp. group g. 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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