2iyt: Difference between revisions

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Revision as of 03:50, 31 March 2008

File:2iyt.gif

, resolution 1.47Å

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Ligands:

Activity:

Shikimate kinase, with EC number 2.7.1.71

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FirstGlance, OCA, PDBsum, RCSB

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save as pdb, mmCIF, xml

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

OverviewOverview

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 StructureAbout this Structure

2IYT is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Mar 31 03:50:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 |PDB= 2iyt |SIZE=350|CAPTION= <scene name='initialview01'>2iyt</scene>, resolution 1.47&Aring;
 |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
-|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
+|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]
+|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=
+|DOMAIN=
+|RELATEDENTRY=
+|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyt OCA], [http://www.ebi.ac.uk/pdbsum/2iyt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iyt RCSB]</span>
 }}
@@ Line 28: / Line 31: @@
 [[Category: Oberschall, A.]]
 [[Category: Strizhov, N.]]
-[[Category: CL]]
 [[Category: amino-acid biosynthesis]]
 [[Category: aromatic amino acid biosynthesis]]
@@ Line 41: / Line 43: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:36 2008''