2egd
From Proteopedia
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|PDB= 2egd |SIZE=350|CAPTION= <scene name='initialview01'>2egd</scene>, resolution 1.80Å | |PDB= 2egd |SIZE=350|CAPTION= <scene name='initialview01'>2egd</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:Ca+Binding+Site+For+Residue+A+302'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Residue+B+303'>AC3</scene> and <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+B+304'>AC4</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:Ca+Binding+Site+For+Residue+A+302'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Residue+B+303'>AC3</scene> and <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+B+304'>AC4</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= S100A13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= S100A13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2egd OCA], [http://www.ebi.ac.uk/pdbsum/2egd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2egd RCSB]</span> | ||
}} | }} | ||
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[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
[[Category: Yonezawa, N.]] | [[Category: Yonezawa, N.]] | ||
| - | [[Category: CA]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
| - | ''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 02:48:41 2008'' |
Revision as of 23:48, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Gene: | S100A13 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human S100A13 in the Ca2+-bound state
Overview
S100A13 is a member of the S100 family of EF-hand-containing calcium-binding proteins. S100A13 plays an important role in the secretion of fibroblast growth factor-1 and interleukin 1 alpha, two pro-angiogenic factors released by the nonclassical endoplasmic reticulum/Golgi-independent secretory pathway. The X-ray crystal structure of human S100A13 at pH 7.5 was determined at 1.8 A resolution. The structure was solved by molecular replacement and was refined to a final R factor of 19.0%. The structure revealed that human S100A13 exists as a homodimer with two calcium ions bound to each protomer. The protomer is composed of four alpha-helices (alpha(1)-alpha(4)), which form a pair of EF-hand motifs. Dimerization occurs by hydrophobic interactions between helices alpha(1) and alpha(4) and by intermolecular hydrogen bonds between residues from helix alpha(1) and the residues between alpha(2) and alpha(3) of both chains. Despite the high similarity of the backbone conformation in each protomer, the crystal structures of human S100A13 at pH 7.5 (this study) and at pH 6.0 [Li et al. (2007), Biochem. Biophys. Res. Commun. 356, 616-621] exhibit recognizable differences in the relative orientation ( approximately 2.5 degrees) of the protomers within the dimer and also remarkable differences in the side-chain conformations of several amino-acid residues.
About this Structure
2EGD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of calcium-bound human S100A13 at pH 7.5 at 1.8 A resolution., Imai FL, Nagata K, Yonezawa N, Nakano M, Tanokura M, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt, 2):70-6. Epub 2008 Jan 31. PMID:18259052
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