This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1gb1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gb1.jpg|left|200px]]<br /><applet load="1gb1" size="350" color="white" frame="true" align="right" caption="1gb1" />
+
[[Image:1gb1.jpg|left|200px]]
-
'''A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G'''<br />
+
 
 +
{{Structure
 +
|PDB= 1gb1 |SIZE=350|CAPTION= <scene name='initialview01'>1gb1</scene>
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G'''
 +
 
==Overview==
==Overview==
Line 16: Line 26:
[[Category: immunoglobulin binding protein]]
[[Category: immunoglobulin binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 18 20:00:47 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:20:44 2008''

Revision as of 09:20, 20 March 2008


PDB ID 1gb1

Drag the structure with the mouse to rotate
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

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

Page seeded by OCA on Thu Mar 20 11:20:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools