1e9p

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[[Image:1e9p.jpg|left|200px]]<br /><applet load="1e9p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e9p.jpg|left|200px]]
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caption="1e9p, resolution 1.70&Aring;" />
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'''CRYSTAL STRUCTURE OF BOVINE CU, ZN SOD TO 1.7 ANGSTROM (3 OF 3)'''<br />
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{{Structure
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|PDB= 1e9p |SIZE=350|CAPTION= <scene name='initialview01'>1e9p</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=CU1:Cu+Binding+Site+For+Residue+A152'>CU1</scene>, <scene name='pdbsite=CU2:Cu+Binding+Site+For+Residue+A153'>CU2</scene>, <scene name='pdbsite=CU3:Cu+Binding+Site+For+Residue+B152'>CU3</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site+For+Residueb153'>ZNB</scene>
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_1.13.11.1 Transferred entry: 1.13.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.1.1 1.13.1.1]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF BOVINE CU, ZN SOD TO 1.7 ANGSTROM (3 OF 3)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1E9P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_1.13.11.1 Transferred entry: 1.13.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.1.1 1.13.1.1] Known structural/functional Sites: <scene name='pdbsite=CU1:Cu+Binding+Site+For+Residue+A152'>CU1</scene>, <scene name='pdbsite=CU2:Cu+Binding+Site+For+Residue+A153'>CU2</scene>, <scene name='pdbsite=CU3:Cu+Binding+Site+For+Residue+B152'>CU3</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site+For+Residueb153'>ZNB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9P OCA].
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1E9P is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9P OCA].
==Reference==
==Reference==
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Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080458 11080458]
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Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080458 11080458]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: superoxide]]
[[Category: superoxide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:52:15 2008''

Revision as of 08:52, 20 March 2008

Image:1e9p.jpg


PDB ID 1e9p

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites: , , and
Ligands: and
Activity: Transferred entry: 1.13.11.1, with EC number 1.13.1.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF BOVINE CU, ZN SOD TO 1.7 ANGSTROM (3 OF 3)


Overview

The structure of the catalytic site in one subunit of bovine CuZn superoxide dismutase is shown to be highly variable. A series of crystal structures at approximately 1.7 A have been determined using data collected from different crystals. Several conformations are observed for the copper site from one of the subunits. These conformations lie between those expected for the Cu(II) and Cu(I) forms of the enzyme and may represent a slow positional rearrangement of the Cu site during the crystallisation process due to the presence of a trace reductant in the mother liquor. These states perhaps indicate some functionally relevant structural steps that ultimately result in the breakage of the imidazolate bridge between the two metal sites.This behaviour is not observed for the second subunit of the dimeric enzyme, which remains in the five-coordinate, distorted square planar geometry in all cases. We suggest that this asymmetric behaviour may be caused by the lack of mobility for the Glu119-Leu142 loop region in the second subunit caused by crystal contacts. This region forms one wall of the active-site cavity, and its mobility has been suggested, via molecular dynamics studies, to be important for the catalytic mechanism.

About this Structure

1E9P is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:11080458

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