From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:3chb.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:3chb.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_3chb| PDB=3chb | SCENE= }} | | {{STRUCTURE_3chb| PDB=3chb | SCENE= }} |
| | | | |
| - | '''CHOLERA TOXIN B-PENTAMER COMPLEXED WITH GM1 PENTASACCHARIDE'''
| + | ===CHOLERA TOXIN B-PENTAMER COMPLEXED WITH GM1 PENTASACCHARIDE=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Crystals of the 61 kDa complex of the cholera toxin B-pentamer with the ganglioside GM1 receptor pentasaccharide diffract to near-atomic resolution. We have refined the crystallographic model for this complex using anisotropic displacement parameters for all atoms to a conventional crystallographic residual R=0.129 for all observed Bragg reflections in the resolution range 22 A to 1.25 A. Remarkably few residues show evidence of discrete conformational disorder. A notable exception is a minority conformation found for the Cys9 side-chain, which implies that the Cys9-Cys86 disulfide linkage is incompletely formed. In all five crystallographically independent instances, the peptide backbone in the region of the receptor-binding site shows evidence of strain, including unusual bond lengths and angles, and a highly non-planar (omega=153.7(7) degrees) peptide group between residues Gln49 and Val50. The location of well-ordered water molecules at the protein surface is notable reproduced among the five crystallographically independent copies of the peptide chain, both at the receptor-binding site and elsewhere. The 5-fold non-crystallographic symmetry of this complex allows an evaluation of the accuracy, reproducibility, and derived error estimates from refinement of large structures at near-atomic resolution. We find that blocked-matrix treatment of parameter covariance underestimates the uncertainty of atomic positions in the final model by approximately 10% relative to estimates based either on full-matrix inversion or on the 5-fold non-crystallographic symmetry.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9753553}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9753553 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9753553}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 27: |
Line 31: |
| | [[Category: Toxin]] | | [[Category: Toxin]] |
| | [[Category: Toxin/receptor complex]] | | [[Category: Toxin/receptor complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:46:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:03:11 2008'' |
Revision as of 05:03, 29 July 2008
Template:STRUCTURE 3chb
CHOLERA TOXIN B-PENTAMER COMPLEXED WITH GM1 PENTASACCHARIDE
Template:ABSTRACT PUBMED 9753553
About this Structure
3CHB is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
Reference
The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site., Merritt EA, Kuhn P, Sarfaty S, Erbe JL, Holmes RK, Hol WG, J Mol Biol. 1998 Oct 9;282(5):1043-59. PMID:9753553
Page seeded by OCA on Tue Jul 29 08:03:11 2008
