2iyt

From Proteopedia

(Difference between revisions)

Revision as of 07:22, 11 July 2018

Shikimate kinase from Mycobacterium tuberculosis in unliganded state, open LID (conf. A)

Structural highlights

2iyt is a 1 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1l4u, 1l4y, 1u8a, 1zyu, 2g1j, 2g1k, 2iyq, 2iyr, 2iys, 2iyu, 2iyv, 2iyw, 2iyx, 2iyy, 2iyz
Activity:	Shikimate kinase, with EC number 2.7.1.71
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AROK_MYCTU] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Oliveira JS, Pinto CA, Basso LA, Santos DS. Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis. Protein Expr Purif. 2001 Aug;22(3):430-5. PMID:11483005 doi:10.1006/prep.2001.1457
↑ Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD. Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis. J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:17020768 doi:10.1016/j.jmb.2006.09.001
↑ Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD. Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis. J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:17020768 doi:10.1016/j.jmb.2006.09.001

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iyt"

@@ Line 1: / Line 1: @@
-==SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)==
+==Shikimate kinase from Mycobacterium tuberculosis in unliganded state, open LID (conf. A)==
 <StructureSection load='2iyt' size='340' side='right' caption='[[2iyt]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l4u|1l4u]], [[1l4y|1l4y]], [[1u8a|1u8a]], [[1zyu|1zyu]], [[2g1j|2g1j]], [[2g1k|2g1k]], [[2iyq|2iyq]], [[2iyr|2iyr]], [[2iys|2iys]], [[2iyu|2iyu]], [[2iyv|2iyv]], [[2iyw|2iyw]], [[2iyx|2iyx]], [[2iyy|2iyy]], [[2iyz|2iyz]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2iyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iyt RCSB], [http://www.ebi.ac.uk/pdbsum/2iyt PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2iyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iyt RCSB], [http://www.ebi.ac.uk/pdbsum/2iyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyt ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iyt_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iyt_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2iyt

From Proteopedia

Revision as of 07:22, 11 July 2018

Shikimate kinase from Mycobacterium tuberculosis in unliganded state, open LID (conf. A)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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