2iyr

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|PDB= 2iyr |SIZE=350|CAPTION= <scene name='initialview01'>2iyr</scene>, resolution 1.98&Aring;
|PDB= 2iyr |SIZE=350|CAPTION= <scene name='initialview01'>2iyr</scene>, resolution 1.98&Aring;
|SITE= <scene name='pdbsite=AC1:Skm+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Skm+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID'>SKM</scene>
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|LIGAND= <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyr OCA], [http://www.ebi.ac.uk/pdbsum/2iyr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iyr RCSB]</span>
}}
}}
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[[Category: Oberschall, A.]]
[[Category: Oberschall, A.]]
[[Category: Strizhov, N.]]
[[Category: Strizhov, N.]]
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[[Category: SKM]]
 
[[Category: amino-acid biosynthesis]]
[[Category: amino-acid biosynthesis]]
[[Category: aromatic amino acid biosynthesis]]
[[Category: aromatic amino acid biosynthesis]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:35 2008''

Revision as of 00:50, 31 March 2008

Image:2iyr.gif


PDB ID 2iyr

Drag the structure with the mouse to rotate
, resolution 1.98Å
Sites:
Ligands:
Activity: Shikimate kinase, with EC number 2.7.1.71
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE


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

2IYR is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from 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:17020768

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