1zfs
From Proteopedia
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|PDB= 1zfs |SIZE=350|CAPTION= <scene name='initialview01'>1zfs</scene> | |PDB= 1zfs |SIZE=350|CAPTION= <scene name='initialview01'>1zfs</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= S100a1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= S100a1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k2h|1K2H]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfs OCA], [http://www.ebi.ac.uk/pdbsum/1zfs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zfs RCSB]</span> | ||
}} | }} | ||
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[[Category: Weber, D J.]] | [[Category: Weber, D J.]] | ||
[[Category: Wright, N T.]] | [[Category: Wright, N T.]] | ||
| - | [[Category: CA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: conformational change]] | [[Category: conformational change]] | ||
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[[Category: x-type 4 helix bundle]] | [[Category: x-type 4 helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:35:23 2008'' |
Revision as of 22:35, 30 March 2008
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| Ligands: | |||||||
| Gene: | S100a1 (Rattus norvegicus) | ||||||
| Related: | 1K2H
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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