2egd

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[[Image:2egd.jpg|left|200px]]<br /><applet load="2egd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2egd.jpg|left|200px]]
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caption="2egd, resolution 1.80&Aring;" />
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'''Crystal structure of human S100A13 in the Ca2+-bound state'''<br />
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{{Structure
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|PDB= 2egd |SIZE=350|CAPTION= <scene name='initialview01'>2egd</scene>, resolution 1.80&Aring;
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|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>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE= S100A13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of human S100A13 in the Ca2+-bound state'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2EGD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EGD OCA].
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2EGD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EGD OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18259052 18259052]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18259052 18259052]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: metal binding protein]]
[[Category: metal binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:29:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:39:47 2008''

Revision as of 14:39, 20 March 2008


PDB ID 2egd

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites: , , and
Ligands:
Gene: S100A13 (Homo sapiens)
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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