1gb1

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==About this Structure==
==About this Structure==
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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].
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1GB1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. 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://www.ncbi.nlm.nih.gov/pubmed/1871600 1871600]
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]]
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[[Category: Streptomyces chryseus]]
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[[Category: Streptomyces griseus]]
[[Category: Clore, G M.]]
[[Category: Clore, G M.]]
[[Category: Gronenborn, A M.]]
[[Category: Gronenborn, A M.]]
[[Category: immunoglobulin binding protein]]
[[Category: immunoglobulin binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 18 13:26:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 18 20:00:47 2008''

Revision as of 18:00, 18 March 2008


1gb1

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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 griseus. 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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