2h34
From Proteopedia
(New page: 200px<br /><applet load="2h34" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h34, resolution 2.800Å" /> '''Apoenzyme crystal s...) |
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| - | [[Image:2h34.gif|left|200px]]<br /><applet load="2h34" size=" | + | [[Image:2h34.gif|left|200px]]<br /><applet load="2h34" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2h34, resolution 2.800Å" /> | caption="2h34, resolution 2.800Å" /> | ||
'''Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE'''<br /> | '''Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The "eukaryotic-like" receptor Ser/Thr protein kinases (STPKs) are | + | The "eukaryotic-like" receptor Ser/Thr protein kinases (STPKs) are candidates for the sensors that mediate environmental adaptations of Mycobacterium tuberculosis (Mtb). To define the mechanisms of regulation and substrate recognition, we determined the crystal structure of the ligand-free, activated kinase domain (KD) of the Mtb STPK, PknE. Remarkably, the PknE KD formed a dimer similar to that first observed in the structure of the ATPgammaS complex of the Mtb paralog, PknB. This structural similarity, which occurs despite little sequence conservation between the PknB and PknE dimer interfaces, supports the idea that dimerization regulates the Mtb receptor STPKs. Insertion of the DFG motif into the ATP-binding site and other conformational differences compared the ATPgammaS:PknB complex suggest that apo-PknE is not pre-organized to bind nucleotides. This structure may represent an inactive conformation stabilized by dimerization or, alternatively, an active conformation that reveals shifts that mediate nucleotide exchange and order substrate binding. |
==About this Structure== | ==About this Structure== | ||
| - | 2H34 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 BR and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http:// | + | 2H34 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=BR:'>BR</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H34 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Gay, L | + | [[Category: Gay, L M.]] |
| - | [[Category: Ng, H | + | [[Category: Ng, H L.]] |
[[Category: BR]] | [[Category: BR]] | ||
[[Category: NA]] | [[Category: NA]] | ||
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[[Category: serine/threonine protein kinase]] | [[Category: serine/threonine protein kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:48 2008'' |
Revision as of 15:37, 21 February 2008
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Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE
Overview
The "eukaryotic-like" receptor Ser/Thr protein kinases (STPKs) are candidates for the sensors that mediate environmental adaptations of Mycobacterium tuberculosis (Mtb). To define the mechanisms of regulation and substrate recognition, we determined the crystal structure of the ligand-free, activated kinase domain (KD) of the Mtb STPK, PknE. Remarkably, the PknE KD formed a dimer similar to that first observed in the structure of the ATPgammaS complex of the Mtb paralog, PknB. This structural similarity, which occurs despite little sequence conservation between the PknB and PknE dimer interfaces, supports the idea that dimerization regulates the Mtb receptor STPKs. Insertion of the DFG motif into the ATP-binding site and other conformational differences compared the ATPgammaS:PknB complex suggest that apo-PknE is not pre-organized to bind nucleotides. This structure may represent an inactive conformation stabilized by dimerization or, alternatively, an active conformation that reveals shifts that mediate nucleotide exchange and order substrate binding.
About this Structure
2H34 is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis., Gay LM, Ng HL, Alber T, J Mol Biol. 2006 Jul 7;360(2):409-20. Epub 2006 May 19. PMID:16762364
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