2iyv: Difference between revisions

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Revision as of 18:35, 20 March 2008

File:2iyv.gif

, resolution 1.35Å

Sites:

Ligands:

and

Activity:

Shikimate kinase, with EC number 2.7.1.71

Coordinates:

save as pdb, mmCIF, xml

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

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

2IYV 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 Thu Mar 20 17:35:12 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2iyv.gif|left|200px]]<br /><applet load="2iyv" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:2iyv.gif|left|200px]]
-caption="2iyv, resolution 1.35&Aring;" />
-'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)'''<br />
+ {{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'-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==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-IYV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYV OCA].
+IYV 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17020768 17020768]
+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]]
@@ Line 33: / Line 42: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:12 2008''