4eqm
From Proteopedia
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| - | [[ | + | ==Structural analysis of Staphylococcus aureus serine/threonine kinase PknB== |
| + | <StructureSection load='4eqm' size='340' side='right' caption='[[4eqm]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4eqm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EQM FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SA1063 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46170 Staphylococcus aureus subsp. aureus])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eqm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eqm RCSB], [http://www.ebi.ac.uk/pdbsum/4eqm PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Effective treatment of infections caused by the bacterium Staphylococcus aureus remains a worldwide challenge, in part due to the constant emergence of new strains that are resistant to antibiotics. The serine/threonine kinase PknB is of particular relevance to the life cycle of S. aureus as it is involved in the regulation of purine biosynthesis, autolysis, and other central metabolic processes of the bacterium. We have determined the crystal structure of the kinase domain of PknB in complex with a non-hydrolyzable analog of the substrate ATP at 3.0 A resolution. Although the purified PknB kinase is active in solution, it crystallized in an inactive, autoinhibited state. Comparison with other bacterial kinases provides insights into the determinants of catalysis, interactions of PknB with ligands, and the pathway of activation. | ||
| - | + | Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB.,Rakette S, Donat S, Ohlsen K, Stehle T PLoS One. 2012;7(6):e39136. Epub 2012 Jun 11. PMID:22701750<ref>PMID:22701750</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Staphylococcus aureus subsp. aureus]] | [[Category: Staphylococcus aureus subsp. aureus]] | ||
[[Category: Rakette, S.]] | [[Category: Rakette, S.]] | ||
Revision as of 08:37, 5 June 2014
Structural analysis of Staphylococcus aureus serine/threonine kinase PknB
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