2iyt: Difference between revisions

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[[Image:2iyt.~~gif~~|left|200px]]

[[Image:2iyt.png|left|200px]]

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~~'''~~SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)~~'''~~

===SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)===

~~==Overview==~~

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The ~~structural mechanism of~~ the ~~catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding~~ to ~~individual steps in~~ the ~~enzymatic reaction~~. ~~The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment~~. ~~Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step~~, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is ~~associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for~~ the ~~second substrate~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17020768}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17020768 is the PubMed ID number.

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==About this Structure==

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[[Category: Shikimate pathway]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 08~~:05:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:28:15 2008''

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-[[Image:2iyt.gif|left|200px]]
+{{Seed}}
+[[Image:2iyt.png|left|200px]]
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 {{STRUCTURE_2iyt|  PDB=2iyt  |  SCENE=  }}
-'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)'''
+===SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)===
-==Overview==
+<!--
-The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.
+The line below this paragraph, {{ABSTRACT_PUBMED_17020768}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17020768 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17020768}}
 ==About this Structure==
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 [[Category: Shikimate pathway]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:05:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:28:15 2008''