1pgx: Difference between revisions
New page: left|200px<br /><applet load="1pgx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pgx, resolution 1.66Å" /> '''THE 1.66 ANGSTROMS X... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1pgx.gif|left|200px]]<br /><applet load="1pgx" size=" | [[Image:1pgx.gif|left|200px]]<br /><applet load="1pgx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pgx, resolution 1.66Å" /> | caption="1pgx, resolution 1.66Å" /> | ||
'''THE 1.66 ANGSTROMS X-RAY STRUCTURE OF THE B2 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G AND COMPARISON TO THE NMR STRUCTURE OF THE B1 DOMAIN'''<br /> | '''THE 1.66 ANGSTROMS X-RAY STRUCTURE OF THE B2 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G AND COMPARISON TO THE NMR STRUCTURE OF THE B1 DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the B2 immunoglobulin-binding domain of streptococcal | The structure of the B2 immunoglobulin-binding domain of streptococcal protein G has been determined at 1.67-A resolution using a combination of single isomorphous replacement (SIR) phasing and manual fitting of the coordinates of the NMR structure of B1 domain of streptococcal protein G [Gronenborn, A. M., et al. (1991) Science 253, 657-661]. The final R value was 0.191 for data between 8.0 and 1.67 A. The structure described here has 13 residues preceding the 57-residue Ig-binding domain and 13 additional residues following it, for a total of 83 residues. The 57-residue binding domain is well-determined in the structure, having an average B factor of 18.0. Only residues 8-77 could be located in the electron density maps, with the ends of the structure fading into disorder. Like the B1 domain, the B2 domain consists of four beta-strands and a single helix lying diagonally across the beta-sheet, with a -1, +3 chi, -1 topology. This small structure is extensively hydrogen-bonded and has a relatively large hydrophobic core. These structural observations may account for the exceptional stability of protein G. A comparison of the B2 domain X-ray structure and the B1 domain NMR structure showed minor differences in the turn between strands and two and a slight displacement of the helix relative to the sheet. Hydrogen bonds between crystallographically related molecules account for most of these differences. | ||
==About this Structure== | ==About this Structure== | ||
1PGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcaceae Streptococcaceae]. Full crystallographic information is available from [http:// | 1PGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcaceae Streptococcaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGX OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Streptococcaceae]] | [[Category: Streptococcaceae]] | ||
[[Category: Achari, A.]] | [[Category: Achari, A.]] | ||
[[Category: Howard, A | [[Category: Howard, A J.]] | ||
[[Category: Whitlow, M.]] | [[Category: Whitlow, M.]] | ||
[[Category: immunoglobulin binding protein]] | [[Category: immunoglobulin binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:42 2008'' | ||
Revision as of 15:28, 21 February 2008
|
THE 1.66 ANGSTROMS X-RAY STRUCTURE OF THE B2 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G AND COMPARISON TO THE NMR STRUCTURE OF THE B1 DOMAIN
OverviewOverview
The structure of the B2 immunoglobulin-binding domain of streptococcal protein G has been determined at 1.67-A resolution using a combination of single isomorphous replacement (SIR) phasing and manual fitting of the coordinates of the NMR structure of B1 domain of streptococcal protein G [Gronenborn, A. M., et al. (1991) Science 253, 657-661]. The final R value was 0.191 for data between 8.0 and 1.67 A. The structure described here has 13 residues preceding the 57-residue Ig-binding domain and 13 additional residues following it, for a total of 83 residues. The 57-residue binding domain is well-determined in the structure, having an average B factor of 18.0. Only residues 8-77 could be located in the electron density maps, with the ends of the structure fading into disorder. Like the B1 domain, the B2 domain consists of four beta-strands and a single helix lying diagonally across the beta-sheet, with a -1, +3 chi, -1 topology. This small structure is extensively hydrogen-bonded and has a relatively large hydrophobic core. These structural observations may account for the exceptional stability of protein G. A comparison of the B2 domain X-ray structure and the B1 domain NMR structure showed minor differences in the turn between strands and two and a slight displacement of the helix relative to the sheet. Hydrogen bonds between crystallographically related molecules account for most of these differences.
About this StructureAbout this Structure
1PGX is a Single protein structure of sequence from Streptococcaceae. Full crystallographic information is available from OCA.
ReferenceReference
1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain., Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M, Biochemistry. 1992 Nov 3;31(43):10449-57. PMID:1420164
Page seeded by OCA on Thu Feb 21 14:28:42 2008