1zfs
From Proteopedia
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'''Solution structure of S100A1 bound to calcium''' | '''Solution structure of S100A1 bound to calcium''' | ||
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[[Category: Weber, D J.]] | [[Category: Weber, D J.]] | ||
[[Category: Wright, N T.]] | [[Category: Wright, N T.]] | ||
| - | [[Category: | + | [[Category: Calcium binding]] |
| - | [[Category: | + | [[Category: Conformational change]] |
| - | [[Category: | + | [[Category: Noncovalent homodimer]] |
| - | [[Category: | + | [[Category: S100]] |
| - | [[Category: | + | [[Category: X-type 4 helix bundle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:34:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:34, 3 May 2008
Solution structure of S100A1 bound to calcium
Overview
S100A1 is an EF-hand-containing Ca(2+)-binding protein that undergoes a conformational change upon binding calcium as is necessary to interact with protein targets and initiate a biological response. To better understand how calcium influences the structure and function of S100A1, the three-dimensional structure of calcium-bound S100A1 was determined by multidimensional NMR spectroscopy and compared to the previously determined structure of apo. In total, 3354 nuclear Overhauser effect-derived distance constraints, 240 dihedral constraints, 160 hydrogen bond constraints, and 362 residual dipolar coupling restraints derived from a series of two-dimensional, three-dimensional, and four-dimensional NMR experiments were used in its structure determination (>21 constraints per residue). As with other dimeric S100 proteins, S100A1 is a symmetric homodimer with helices 1, 1', 4, and 4' associating into an X-type four-helix bundle at the dimer interface. Within each subunit there are four alpha-helices and a short antiparallel beta-sheet typical of two helix-loop-helix EF-hand calcium-binding domains. The addition of calcium did not change the interhelical angle of helices 1 and 2 in the pseudo EF-hand significantly; however, there was a large reorientation of helix 3 in the typical EF-hand. The large conformational change exposes a hydrophobic cleft, defined by residues in the hinge region, the C terminus, and regions of helix 3, which are important for the interaction between S100A1 and a peptide (TRTK-12) derived from the actin-capping protein CapZ.
About this Structure
1ZFS is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The three-dimensional solution structure of Ca(2+)-bound S100A1 as determined by NMR spectroscopy., Wright NT, Varney KM, Ellis KC, Markowitz J, Gitti RK, Zimmer DB, Weber DJ, J Mol Biol. 2005 Oct 21;353(2):410-26. PMID:16169012 Page seeded by OCA on Sat May 3 17:34:14 2008
