4esq

From Proteopedia

(Difference between revisions)

Revision as of 04:12, 7 October 2022

Crystal structure of the extracellular domain of PknH from Mycobacterium tuberculosis

Structural highlights

4esq is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PKNH_MYCTU May regulate bacterial growth in response to external signals to facilitate adaptation to the host environment. In vitro, phosphorylates several substrates such as EmbR, DevR (DosR), DacB1 and Rv0681.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Since their discovery over 20years ago, eukaryotic-like transmembrane receptor Ser/Thr protein kinases (STPKs) have been shown to play critical roles in the virulence, growth, persistence, and reactivation of many bacteria. Information regarding the signals transmitted by these proteins, however, remains scarce. To enhance understanding of the basis for STPK receptor signaling, we determined the 1.7-A-resolution crystal structure of the extracellular sensor domain of the Mycobacterium tuberculosis receptor STPK, PknH (Rv1266c). The PknH sensor domain adopts an unanticipated fold containing two intramolecular disulfide bonds and a large hydrophobic and polar cleft. The residues lining the cleft and those surrounding the disulfide bonds are conserved. These results suggest that PknH binds a small-molecule ligand that signals by changing the location or quaternary structure of the kinase domain.

Structure of the Sensor Domain of Mycobacterium tuberculosis PknH Receptor Kinase Reveals a Conserved Binding Cleft.,Cavazos A, Prigozhin DM, Alber T J Mol Biol. 2012 Jun 20. PMID:22727744^[8]

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

References

↑ Molle V, Kremer L, Girard-Blanc C, Besra GS, Cozzone AJ, Prost JF. An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis. Biochemistry. 2003 Dec 30;42(51):15300-9. doi: 10.1021/bi035150b. PMID:14690440 doi:http://dx.doi.org/10.1021/bi035150b
↑ Sharma K, Chandra H, Gupta PK, Pathak M, Narayan A, Meena LS, D'Souza RC, Chopra P, Ramachandran S, Singh Y. PknH, a transmembrane Hank's type serine/threonine kinase from Mycobacterium tuberculosis is differentially expressed under stress conditions. FEMS Microbiol Lett. 2004 Apr 1;233(1):107-13. doi: 10.1016/j.femsle.2004.01.045. PMID:15043876 doi:http://dx.doi.org/10.1016/j.femsle.2004.01.045
↑ Papavinasasundaram KG, Chan B, Chung JH, Colston MJ, Davis EO, Av-Gay Y. Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB/c mice. J Bacteriol. 2005 Aug;187(16):5751-60. doi: 10.1128/JB.187.16.5751-5760.2005. PMID:16077122 doi:http://dx.doi.org/10.1128/JB.187.16.5751-5760.2005
↑ Sharma K, Gupta M, Pathak M, Gupta N, Koul A, Sarangi S, Baweja R, Singh Y. Transcriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein, EmbR, in vivo. J Bacteriol. 2006 Apr;188(8):2936-44. PMID:16585755 doi:http://dx.doi.org/10.1128/JB.188.8.2936-2944.2006
↑ Sharma K, Gupta M, Krupa A, Srinivasan N, Singh Y. EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis. FEBS J. 2006 Jun;273(12):2711-21. PMID:16817899 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05289.x
↑ Zheng X, Papavinasasundaram KG, Av-Gay Y. Novel substrates of Mycobacterium tuberculosis PknH Ser/Thr kinase. Biochem Biophys Res Commun. 2007 Mar 30;355(1):162-8. doi:, 10.1016/j.bbrc.2007.01.122. Epub 2007 Jan 30. PMID:17286964 doi:http://dx.doi.org/10.1016/j.bbrc.2007.01.122
↑ Chao JD, Papavinasasundaram KG, Zheng X, Chavez-Steenbock A, Wang X, Lee GQ, Av-Gay Y. Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis. J Biol Chem. 2010 Sep 17;285(38):29239-46. doi: 10.1074/jbc.M110.132894. Epub, 2010 Jul 14. PMID:20630871 doi:http://dx.doi.org/10.1074/jbc.M110.132894
↑ Cavazos A, Prigozhin DM, Alber T. Structure of the Sensor Domain of Mycobacterium tuberculosis PknH Receptor Kinase Reveals a Conserved Binding Cleft. J Mol Biol. 2012 Jun 20. PMID:22727744 doi:10.1016/j.jmb.2012.06.011

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4esq"

Categories: Large Structures | Mycobacterium tuberculosis H37Rv | Alber T | Cavazos A | Prigozhin DM

@@ Line 1: / Line 1: @@
 ==Crystal structure of the extracellular domain of PknH from Mycobacterium tuberculosis==
-<StructureSection load='4esq' size='340' side='right' caption='[[4esq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+<StructureSection load='4esq' size='340' side='right'caption='[[4esq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4esq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ESQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ESQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4esq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ESQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ESQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pknH, Rv1266c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4esq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4esq OCA], [https://pdbe.org/4esq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4esq RCSB], [https://www.ebi.ac.uk/pdbsum/4esq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4esq ProSAT]</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=4esq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4esq OCA], [http://pdbe.org/4esq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4esq RCSB], [http://www.ebi.ac.uk/pdbsum/4esq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4esq ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PKNH_MYCTU PKNH_MYCTU] May regulate bacterial growth in response to external signals to facilitate adaptation to the host environment. In vitro, phosphorylates several substrates such as EmbR, DevR (DosR), DacB1 and Rv0681.<ref>PMID:14690440</ref> <ref>PMID:15043876</ref> <ref>PMID:16077122</ref> <ref>PMID:16585755</ref> <ref>PMID:16817899</ref> <ref>PMID:17286964</ref> <ref>PMID:20630871</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 4esq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Myctu]]
+[[Category: Large Structures]]
-[[Category: Alber, T]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Cavazos, A]]
+[[Category: Alber T]]
-[[Category: Prigozhin, D M]]
+[[Category: Cavazos A]]
-[[Category: Membrane]]
+[[Category: Prigozhin DM]]
-[[Category: Receptor kinase]]
-[[Category: Transferase]]

4esq

From Proteopedia

Revision as of 04:12, 7 October 2022

Crystal structure of the extracellular domain of PknH from Mycobacterium tuberculosis

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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