View source for 2iyv

[[Image:2iyv.gif|left|200px]]

 {{Structure
|PDB= 2iyv |SIZE=350|CAPTION= <scene name='initialview01'>2iyv</scene>, resolution 1.35&Aring;
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] 
|GENE= 
}}

'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)'''


==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.

==About this Structure==
2IYV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYV OCA]. 

==Reference==
Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis., Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD, J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17020768 17020768]
[[Category: Mycobacterium tuberculosis]]
[[Category: Shikimate kinase]]
[[Category: Single protein]]
[[Category: Bartunik, H D.]]
[[Category: Bourenkov, G P.]]
[[Category: Hartmann, M D.]]
[[Category: Oberschall, A.]]
[[Category: Strizhov, N.]]
[[Category: ADP]]
[[Category: CL]]
[[Category: amino-acid biosynthesis]]
[[Category: aromatic amino acid biosynthesis]]
[[Category: atp-binding]]
[[Category: kinase]]
[[Category: magnesium]]
[[Category: metal-binding]]
[[Category: nucleotide-binding]]
[[Category: p-loop kinase]]
[[Category: shikimate kinase]]
[[Category: shikimate pathway]]
[[Category: transferase]]

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