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2gb1
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1gb1|1GB1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb1 OCA], [http://www.ebi.ac.uk/pdbsum/2gb1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gb1 RCSB]</span> | ||
}} | }} | ||
| Line 16: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2GB1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2GB1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB1 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: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Streptococcus sp. group g]] | ||
[[Category: Clore, G M.]] | [[Category: Clore, G M.]] | ||
[[Category: Gronenborn, A M.]] | [[Category: Gronenborn, A M.]] | ||
[[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 Mon Mar 31 03:14:16 2008'' |
Revision as of 00:14, 31 March 2008
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| Related: | 1GB1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
2GB1 is a Single protein structure of sequence from Bacteria. 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
Page seeded by OCA on Mon Mar 31 03:14:16 2008
