1c97
From Proteopedia
(New page: 200px<br /><applet load="1c97" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c97, resolution 1.98Å" /> '''S642A:ISOCITRATE COM...) |
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| - | [[Image:1c97.gif|left|200px]]<br /><applet load="1c97" size=" | + | [[Image:1c97.gif|left|200px]]<br /><applet load="1c97" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c97, resolution 1.98Å" /> | caption="1c97, resolution 1.98Å" /> | ||
'''S642A:ISOCITRATE COMPLEX OF ACONITASE'''<br /> | '''S642A:ISOCITRATE COMPLEX OF ACONITASE'''<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== | ||
| - | 1C97 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SF4, O and ICT 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:// | + | 1C97 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=O:'>O</scene> and <scene name='pdbligand=ICT:'>ICT</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=1C97 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[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: O]] | [[Category: O]] | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:43 2008'' |
Revision as of 10:03, 21 February 2008
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S642A:ISOCITRATE COMPLEX OF ACONITASE
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
1C97 is a Single protein structure of sequence from Bos taurus with , and as ligands. 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 12:03:43 2008
Categories: Aconitate hydratase | Bos taurus | Single protein | Lauble, H. | Lloyd, S J. | Prasad, G S. | Stout, C D. | ICT | O | SF4 | 3d-structure | 4fe-4s | Iron-sulfur | Lyase | Mitochondrion | Transit peptide | Tricarboxylic acid cycle
