1b0m: Difference between revisions

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[[Image:1b0m.~~gif~~|left|200px]]

[[Image:1b0m.png|left|200px]]

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~~'''~~ACONITASE R644Q:FLUOROCITRATE COMPLEX~~'''~~

===ACONITASE R644Q:FLUOROCITRATE COMPLEX===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_10631981}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10631981 is the PubMed ID number.

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==About this Structure==

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[[Category: Fluorocitrate complex]]

[[Category: Hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:55:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:59:35 2008''

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-[[Image:1b0m.gif|left|200px]]
+{{Seed}}
+[[Image:1b0m.png|left|200px]]
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 {{STRUCTURE_1b0m|  PDB=1b0m  |  SCENE=  }}
-'''ACONITASE R644Q:FLUOROCITRATE COMPLEX'''
+===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 --&gt; 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10631981}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10631981 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10631981}}
 ==About this Structure==
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 [[Category: Fluorocitrate complex]]
 [[Category: Hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:55:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:59:35 2008''