1bdd: Difference between revisions

Revision as of 18:53, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bdd.png

Template:STRUCTURE 1bdd

STAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURESTAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 1390743

About this StructureAbout this Structure

1BDD is a Single protein structure of sequence from Staphylococcus aureus. Full experimental information is available from OCA.

ReferenceReference

Three-dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures., Gouda H, Torigoe H, Saito A, Sato M, Arata Y, Shimada I, Biochemistry. 1992 Oct 13;31(40):9665-72. PMID:1390743

Page seeded by OCA on Mon Jun 30 18:53:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bdd.gif|left|200px]]
+{{Seed}}
+[[Image:1bdd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bdd|  PDB=1bdd  |  SCENE=  }}
-'''STAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''
+===STAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE===
-==Overview==
+<!--
-The three-dimensional solution structure of the recombinant B domain (FB) of staphylococcal protein A, which specifically binds to the Fc portion of immunoglobulin G, was determined by NMR spectroscopy and hybrid distance geometry-dynamical simulated annealing calculations. On the basis of 692 experimental constraints including 587 distance constraints obtained from the nuclear Overhauser effect (NOE), 57 torsion angle (phi, chi 1) constraints, and 48 constraints associated with 24 hydrogen bonds, a total of 10 converged structures of FB were obtained. The atomic root mean square difference among the 10 converged structures is 0.52 +/- 0.10 A for the backbone atoms and 0.98 +/- 0.08 A for all heavy atoms (excluding the N-terminal segment from Thr1 to Glu9 and the C-terminal segment from Gln56 to Ala60, which are partially disordered). FB is composed of a bundle of three alpha-helices, i.e., helix I (Gln10-His19), helix II (Glu25-Asp37), and helix III (Ser42-Ala55). Helix II and helix III are antiparallel to each other, whereas the long axis of helix I is tilted at an angle of about 30 degrees with respect to those of helix II and helix III. Most of the hydrophobic residues of FB are buried in the interior of the bundle of the three helices. It is suggested that the buried hydrophobic residues form a hydrophobic core, contributing to the stability of FB.(ABSTRACT TRUNCATED AT 250 WORDS)
+The line below this paragraph, {{ABSTRACT_PUBMED_1390743}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1390743 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1390743}}
 ==About this Structure==
-BDD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDD OCA].
+BDD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDD OCA].
 ==Reference==
@@ Line 34: / Line 38: @@
 [[Category: Signal]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:22:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:53:22 2008''