|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5nod' size='340' side='right'caption='[[5nod]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5nod' size='340' side='right'caption='[[5nod]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NOD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NOD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stkP, pkn2, spr1577 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 STRR6])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=5nod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nod OCA], [https://pdbe.org/5nod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nod RCSB], [https://www.ebi.ac.uk/pdbsum/5nod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nod 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=5nod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nod OCA], [http://pdbe.org/5nod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nod RCSB], [http://www.ebi.ac.uk/pdbsum/5nod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nod ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STKP_STRR6 STKP_STRR6]] Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to constitute a functional signaling couple in vivo.<ref>PMID:22211696</ref> <ref>PMID:22431591</ref> | + | [https://www.uniprot.org/uniprot/STKP_STRR6 STKP_STRR6] Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to constitute a functional signaling couple in vivo.<ref>PMID:22211696</ref> <ref>PMID:22431591</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Streptococcus pneumoniae R6]] |
| - | [[Category: Strr6]]
| + | [[Category: Galisson F]] |
| - | [[Category: Galisson, F]] | + | [[Category: Gouet P]] |
| - | [[Category: Gouet, P]] | + | [[Category: Grangeasse C]] |
| - | [[Category: Grangeasse, C]] | + | [[Category: Gueguen-Chaignon V]] |
| - | [[Category: Gueguen-Chaignon, V]] | + | [[Category: Zucchini L]] |
| - | [[Category: Zucchini, L]] | + | |
| - | [[Category: Extracellular domain]]
| + | |
| - | [[Category: Pasta]]
| + | |
| - | [[Category: Ser/thr kinase]]
| + | |
| - | [[Category: Streptococcus pneumoniae]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
STKP_STRR6 Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to constitute a functional signaling couple in vivo.[1] [2]
Publication Abstract from PubMed
Eukaryotic-like serine/threonine kinases (eSTKs) with extracellular PASTA repeats are key membrane regulators of bacterial cell division. How PASTA repeats govern eSTK activation and function remains elusive. Using evolution- and structural-guided approaches combined with cell imaging, we disentangle the role of each PASTA repeat of the eSTK StkP from Streptococcus pneumoniae. While the three membrane-proximal PASTA repeats behave as interchangeable modules required for the activation of StkP independently of cell wall binding, they also control the septal cell wall thickness. In contrast, the fourth and membrane-distal PASTA repeat directs StkP localization at the division septum and encompasses a specific motif that is critical for final cell separation through interaction with the cell wall hydrolase LytB. We propose a model in which the extracellular four-PASTA domain of StkP plays a dual function in interconnecting the phosphorylation of StkP endogenous targets along with septal cell wall remodelling to allow cell division of the pneumococcus.
PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae.,Zucchini L, Mercy C, Garcia PS, Cluzel C, Gueguen-Chaignon V, Galisson F, Freton C, Guiral S, Brochier-Armanet C, Gouet P, Grangeasse C Nat Microbiol. 2017 Dec 4. pii: 10.1038/s41564-017-0069-3. doi:, 10.1038/s41564-017-0069-3. PMID:29203882[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fleurie A, Cluzel C, Guiral S, Freton C, Galisson F, Zanella-Cleon I, Di Guilmi AM, Grangeasse C. Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae. Mol Microbiol. 2012 Feb;83(4):746-58. doi: 10.1111/j.1365-2958.2011.07962.x. Epub, 2012 Jan 11. PMID:22211696 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07962.x
- ↑ Beilharz K, Novakova L, Fadda D, Branny P, Massidda O, Veening JW. Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP. Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):E905-13. doi:, 10.1073/pnas.1119172109. Epub 2012 Mar 19. PMID:22431591 doi:http://dx.doi.org/10.1073/pnas.1119172109
- ↑ Zucchini L, Mercy C, Garcia PS, Cluzel C, Gueguen-Chaignon V, Galisson F, Freton C, Guiral S, Brochier-Armanet C, Gouet P, Grangeasse C. PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae. Nat Microbiol. 2017 Dec 4. pii: 10.1038/s41564-017-0069-3. doi:, 10.1038/s41564-017-0069-3. PMID:29203882 doi:http://dx.doi.org/10.1038/s41564-017-0069-3
|
