3gb1
From Proteopedia
(Difference between revisions)
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==STRUCTURES OF B1 DOMAIN OF STREPTOCOCCAL PROTEIN G== | ==STRUCTURES OF B1 DOMAIN OF STREPTOCOCCAL PROTEIN G== | ||
- | <StructureSection load='3gb1' size='340' side='right' caption='[[3gb1]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''> | + | <StructureSection load='3gb1' size='340' side='right'caption='[[3gb1]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3gb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strsg Strsg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GB1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3gb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strsg Strsg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GB1 FirstGlance]. <br> | ||
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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=3gb1 ConSurf]. | </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=3gb1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C). | ||
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+ | A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.,Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM Science. 1991 Aug 9;253(5020):657-61. PMID:1871600<ref>PMID:1871600</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 3gb1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Protein G|Protein G]] | *[[Protein G|Protein G]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Strsg]] | [[Category: Strsg]] | ||
[[Category: Clore, G M]] | [[Category: Clore, G M]] | ||
[[Category: Immunoglobulin binding protein]] | [[Category: Immunoglobulin binding protein]] |
Revision as of 07:13, 27 November 2019
STRUCTURES OF B1 DOMAIN OF STREPTOCOCCAL PROTEIN G
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