4ne2
From Proteopedia
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| - | + | ==Pantothenamide-bound Pantothenate Kinase from Klebsiella pneumoniae== | |
| - | + | <StructureSection load='4ne2' size='340' side='right' caption='[[4ne2]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4ne2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Klep3 Klep3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NE2 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SH2:(R)-N-(3-((2-(BENZO[D][1,3]DIOXOL-5-YL)ETHYL)AMINO)-3-OXOPROPYL)-2,4-DIHYDROXY-3,3-DIMETHYLBUTANAMIDE'>SH2</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nb4|4nb4]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coaA, KPK_5321, UUU_44690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=507522 KLEP3])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantothenate_kinase Pantothenate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33] </span></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=4ne2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ne2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ne2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ne2 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pantothenate kinase (PanK) is the rate-limiting enzyme in Coenzyme A biosynthesis, catalyzing the ATP-dependent phosphorylation of pantothenate. We solved the co-crystal structures of PanKs from Staphylococcus aureus (SaPanK) and Klebsiella pneumonia (KpPanK) with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide (N354-Pan). Two different N354-Pan conformers interact with polar/nonpolar mixed residues in SaPanK and aromatic residues in KpPanK. Additionally, phosphorylated N354-Pan is found at the closed active site of SaPanK but not at the open active site of KpPanK, suggesting an exchange of the phosphorylated product with a new N354-Pan only in KpPanK. Together, pantothenamides conformational flexibility and binding pocket are two key considerations for selective compound design. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. | ||
| - | + | Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumonia and Staphylococcus aureus.,Hughes SJ, Antoshchenko T, Kim KP, Smil D, Park HW Proteins. 2014 Jan 28. doi: 10.1002/prot.24524. PMID:24470271<ref>PMID:24470271</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Pantothenate kinase|Pantothenate kinase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Klep3]] | ||
[[Category: Pantothenate kinase]] | [[Category: Pantothenate kinase]] | ||
[[Category: Antoshchenko, T.]] | [[Category: Antoshchenko, T.]] | ||
Revision as of 05:13, 25 June 2014
Pantothenamide-bound Pantothenate Kinase from Klebsiella pneumoniae
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