1b0m
From Proteopedia
(New page: 200px<br /><applet load="1b0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0m, resolution 2.50Å" /> '''ACONITASE R644Q:FLUO...) |
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| - | [[Image:1b0m.gif|left|200px]]<br /><applet load="1b0m" size=" | + | [[Image:1b0m.gif|left|200px]]<br /><applet load="1b0m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b0m, resolution 2.50Å" /> | caption="1b0m, resolution 2.50Å" /> | ||
'''ACONITASE R644Q:FLUOROCITRATE COMPLEX'''<br /> | '''ACONITASE R644Q:FLUOROCITRATE COMPLEX'''<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== | ||
| - | 1B0M 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 FLC and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1B0M 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=FLC:'>FLC</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1ATQ. 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=1B0M 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: FLC]] | [[Category: FLC]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:14 2008'' |
Revision as of 09:50, 21 February 2008
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ACONITASE R644Q:FLUOROCITRATE COMPLEX
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
1B0M is a Single protein structure of sequence from Sus scrofa with and as ligands. This structure supersedes the now removed PDB entry 1ATQ. 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
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