2IYQ

Shikimate kinase from Mycobacterium tuberculosis in complex with shikimate and ADP

Summary for 2IYQ

• Entry DOI: 10.2210/pdb2iyq/pdb
• Related: 1L4U 1L4Y 1U8A 1ZYU 2G1J 2G1K 2IYR 2IYS 2IYT 2IYU 2IYV 2IYW 2IYX 2IYY 2IYZ
• Descriptor: SHIKIMATE KINASE, (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: transferase, aromatic amino acid biosynthesis, kinase, magnesium, p-loop kinase, metal-binding, shikimate kinase, shikimate pathway, nucleotide-binding, amino-acid biosynthesis, atp-binding
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 1
• Total formula weight: 20548.81

Authors

Hartmann, M.D.,Bourenkov, G.P.,Oberschall, A.,Strizhov, N.,Bartunik, H.D. (deposition date: 2006-07-21, release date: 2006-10-11, Last modification date: 2023-12-13)

Primary citation

Hartmann, M.D.,Bourenkov, G.P.,Oberschall, A.,Strizhov, N.,Bartunik, H.D.
Mechanism of Phosphoryl Transfer Catalyzed by Shikimate Kinase from Mycobacterium Tuberculosis.
J.Mol.Biol., 364:411-, 2006

PubMed Abstract: 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.

PubMed: 17020768
DOI: 10.1016/J.JMB.2006.09.001

Experimental method

X-RAY DIFFRACTION (1.8 Å)