6acn

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[[Image:6acn.gif|left|200px]]<br /><applet load="6acn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:6acn.gif|left|200px]]
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caption="6acn, resolution 2.5&Aring;" />
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'''STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE (4FE-4S) CLUSTER IN THE CRYSTAL'''<br />
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{{Structure
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|PDB= 6acn |SIZE=350|CAPTION= <scene name='initialview01'>6acn</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=TRC:TRICARBALLYLIC ACID'>TRC</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3]
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|GENE=
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}}
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'''STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE (4FE-4S) CLUSTER IN THE CRYSTAL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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6ACN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=TRC:'>TRC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACN OCA].
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6ACN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACN OCA].
==Reference==
==Reference==
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Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal., Robbins AH, Stout CD, Proc Natl Acad Sci U S A. 1989 May;86(10):3639-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2726740 2726740]
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Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal., Robbins AH, Stout CD, Proc Natl Acad Sci U S A. 1989 May;86(10):3639-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2726740 2726740]
[[Category: Aconitate hydratase]]
[[Category: Aconitate hydratase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: lyase(carbon-oxygen)]]
[[Category: lyase(carbon-oxygen)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:16:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:13:07 2008''

Revision as of 17:13, 20 March 2008


PDB ID 6acn

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , and
Activity: Aconitate hydratase, with EC number 4.2.1.3
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE (4FE-4S) CLUSTER IN THE CRYSTAL


Overview

The structure of activated pig heart aconitase [citrate(isocitrate) hydro-lyase, EC 4.2.1.3] containing a [4Fe-4S] cluster has been refined at 2.5-A resolution to a crystallographic residual of 18.2%. Comparison of this structure to the recently determined 2.1-A resolution structure of the inactive enzyme containing a [3Fe-4S] cluster, by difference Fourier analysis, shows that upon activation iron is inserted into the structure isomorphously. The common atoms of the [3Fe-4S] and [4Fe-4S] cores agree within 0.1 A; the three common cysteinyl S gamma ligand atoms agree within 0.25 A. The fourth ligand of the Fe inserted into the [3Fe-4S] cluster is a water or hydroxyl from solvent, consistent with the absence of a free cysteine ligand in the enzyme active site cleft and the isomorphism of the two structures. A water molecule occupies a similar site in the crystal structure of the inactive enzyme.

About this Structure

6ACN is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal., Robbins AH, Stout CD, Proc Natl Acad Sci U S A. 1989 May;86(10):3639-43. PMID:2726740

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