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| | ==Octameric kinase domain of the E. coli tyrosine kinase Wzc with bound ADP== | | ==Octameric kinase domain of the E. coli tyrosine kinase Wzc with bound ADP== |
| - | <StructureSection load='3la6' size='340' side='right' caption='[[3la6]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='3la6' size='340' side='right'caption='[[3la6]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3la6]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LA6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3la6]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LA6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2060, JW2045, wzc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3la6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3la6 OCA], [http://pdbe.org/3la6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3la6 RCSB], [http://www.ebi.ac.uk/pdbsum/3la6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3la6 ProSAT]</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=3la6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3la6 OCA], [https://pdbe.org/3la6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3la6 RCSB], [https://www.ebi.ac.uk/pdbsum/3la6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3la6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/WZC_ECOLI WZC_ECOLI]] Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium. Phosphorylates udg. | + | [https://www.uniprot.org/uniprot/WZC_ECOLI WZC_ECOLI] Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium. Phosphorylates udg. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Tyrosine kinase|Tyrosine kinase]] | + | *[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Bechet, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Grangeasse, C]] | + | [[Category: Bechet E]] |
| - | [[Category: Gruszczyk, J]] | + | [[Category: Grangeasse C]] |
| - | [[Category: Gueguen-Chaignon, V]] | + | [[Category: Gruszczyk J]] |
| - | [[Category: Nessler, S]] | + | [[Category: Gueguen-Chaignon V]] |
| - | [[Category: Vigouroux, A]] | + | [[Category: Nessler S]] |
| - | [[Category: Bacterial protein kinase]]
| + | [[Category: Vigouroux A]] |
| - | [[Category: Exopolysaccharide synthesis]]
| + | |
| - | [[Category: Intermolecular phosphorylation]]
| + | |
| - | [[Category: Nucleotide binding domain]]
| + | |
| - | [[Category: Oligomerization]]
| + | |
| - | [[Category: P-loop protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Walker a motif]]
| + | |
| Structural highlights
Function
WZC_ECOLI Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium. Phosphorylates udg.
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
Capsular polysaccharides are well-established virulence factors of pathogenic bacteria. Their biosynthesis and export are regulated within the transmembrane polysaccharide assembly machinery by the autophosphorylation of atypical tyrosine-kinases, named BY-kinases. However, the accurate functioning of these tyrosine-kinases remains unknown. Here, we report the crystal structure of the non-phosphorylated cytoplasmic domain of the tyrosine-kinase Wzc from Escherichia coli in complex with ADP showing that it forms a ring-shaped octamer. Mutational analysis demonstrates that a conserved EX(2)RX(2)R motif involved in subunit interactions is essential for polysaccharide export. We also elucidate the role of a putative internal regulatory tyrosine and we show that BY-kinases from proteobacteria autophosphorylate on their C-terminal tyrosine cluster via a single step intermolecular mechanism. This structure-function analysis also allows us to demonstrate that two different parts of a conserved basic region called the RK-cluster are essential for polysaccharide export and for kinase activity, respectively. Based on these data, we revisit the dichotomy made between BY-kinases from proteobacteria and firmicutes and we propose a unique process of oligomerization and phosphorylation. We also reassess the function of BY-kinases in the capsular polysaccharide assembly machinery.
Identification of structural and molecular determinants of the tyrosine-kinase Wzc and implications in capsular polysaccharide export.,Bechet E, Gruszczyk J, Terreux R, Gueguen-Chaignon V, Vigouroux A, Obadia B, Cozzone AJ, Nessler S, Grangeasse C Mol Microbiol. 2010 Jul 13. PMID:20633230[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bechet E, Gruszczyk J, Terreux R, Gueguen-Chaignon V, Vigouroux A, Obadia B, Cozzone AJ, Nessler S, Grangeasse C. Identification of structural and molecular determinants of the tyrosine-kinase Wzc and implications in capsular polysaccharide export. Mol Microbiol. 2010 Jul 13. PMID:20633230 doi:10.1111/j.1365-2958.2010.07291.x
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