1b0j
From Proteopedia
(New page: 200px<br /><applet load="1b0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0j, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1b0j.gif|left|200px]]<br /><applet load="1b0j" size=" | + | [[Image:1b0j.gif|left|200px]]<br /><applet load="1b0j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b0j, resolution 2.50Å" /> | caption="1b0j, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF ACONITASE WITH ISOCITRATE'''<br /> | '''CRYSTAL STRUCTURE OF ACONITASE WITH ISOCITRATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) | + | The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism. |
==About this Structure== | ==About this Structure== | ||
| - | 1B0J 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 SF4 and ICT as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1B0J 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=SF4:'>SF4</scene> and <scene name='pdbligand=ICT:'>ICT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1AR3. 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=1B0J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Lauble, H.]] | [[Category: Lauble, H.]] | ||
| - | [[Category: Lloyd, S | + | [[Category: Lloyd, S J.]] |
| - | [[Category: Prasad, G | + | [[Category: Prasad, G S.]] |
| - | [[Category: Stout, C | + | [[Category: Stout, C D.]] |
[[Category: ICT]] | [[Category: ICT]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:15 2008'' |
Revision as of 09:50, 21 February 2008
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CRYSTAL STRUCTURE OF ACONITASE WITH ISOCITRATE
Overview
The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.
About this Structure
1B0J is a Single protein structure of sequence from Sus scrofa with and as ligands. This structure supersedes the now removed PDB entry 1AR3. Active as Aconitate hydratase, with EC number 4.2.1.3 Full crystallographic information is available from OCA.
Reference
The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex., Lloyd SJ, Lauble H, Prasad GS, Stout CD, Protein Sci. 1999 Dec;8(12):2655-62. PMID:10631981
Page seeded by OCA on Thu Feb 21 11:50:15 2008
Categories: Aconitate hydratase | Single protein | Sus scrofa | Lauble, H. | Lloyd, S J. | Prasad, G S. | Stout, C D. | ICT | SF4 | Complex | Lyase | Transit peptide
