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.


1xyd

From Proteopedia

Revision as of 04:18, 21 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1xyd

Drag the structure with the mouse to rotate

NMR Solution Structure of Rat Zinc-Calcium-S100B, 20 Structures

Overview

The EF-hand calcium-binding protein S100B also binds one zinc ion per, subunit with a relatively high affinity (K(d) approximately 90 nM) [Wilder, et al., (2003) Biochemistry 42, 13410-13421]. In this study, the, structural characterization of zinc binding to calcium-loaded S100B was, examined using high-resolution NMR techniques, including structural, characterization of this complex in solution at atomic resolution. As with, other S100 protein structures, the quaternary structure of, Zn(2+)-Ca(2+)-bound S100B was found to be dimeric with helices H1, H1', H4, and H4' forming an X-type four-helix bundle at the dimer interface., NMR data together with mutational analyses are consistent with Zn(2+), coordination arising from His-15 and His-25 of one S100B subunit and from, His-85 and Glu-89 of the other subunit. The addition of Zn(2+) was also, found to extend helices H4 and H4' three to four residues similar to what, was previously observed with the binding of target proteins to S100B., Furthermore, a kink in helix 4 was observed in Zn(2+)-Ca(2+)-bound S100B, that is not in Ca(2+)-bound S100B. These structural changes upon, Zn(2+)-binding could explain the 5-fold increase in affinity that, Zn(2+)-Ca(2+)-bound S100B has for peptide targets such as the TRTK peptide, versus Ca(2+)-bound S100B. There are also changes in the relative, positioning of the two EF-hand calcium-binding domains and the respective, helices comprising these EF-hands. Changes in conformation such as these, could contribute to the order of magnitude higher affinity that S100B has, for calcium in the presence of Zn(2+).

About this Structure

1XYD is a Single protein structure of sequence from Rattus norvegicus with CA and ZN as ligands. Full crystallographic information is available from OCA.

Reference

Solution structure of zinc- and calcium-bound rat S100B as determined by nuclear magnetic resonance spectroscopy., Wilder PT, Varney KM, Weiss MB, Gitti RK, Weber DJ, Biochemistry. 2005 Apr 19;44(15):5690-702. PMID:15823027

Page seeded by OCA on Wed Nov 21 06:25:59 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools