1gb1
From Proteopedia
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| - | [[Image:1gb1.jpg|left|200px]]<br /><applet load="1gb1" size="350" color="white" frame="true" align="right" | + | [[Image:1gb1.jpg|left|200px]]<br /><applet load="1gb1" size="350" color="white" frame="true" align="right" caption="1gb1" /> |
| - | caption="1gb1" /> | + | |
'''A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G'''<br /> | '''A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GB1 is a [ | + | 1GB1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_chryseus Streptomyces chryseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB1 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1871600 1871600] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces chryseus]] | [[Category: Streptomyces chryseus]] | ||
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[[Category: immunoglobulin binding protein]] | [[Category: immunoglobulin binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 18 13:26:01 2008'' |
Revision as of 11:26, 18 March 2008
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A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G
Overview
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).
About this Structure
1GB1 is a Single protein structure of sequence from Streptomyces chryseus. Full crystallographic information is available from OCA.
Reference
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
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