4r7b: Difference between revisions
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==Crystal structure of pneumococcal LicA in complex with choline== | |||
<StructureSection load='4r7b' size='340' side='right'caption='[[4r7b]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r7b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R7B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></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=4r7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r7b OCA], [https://pdbe.org/4r7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r7b RCSB], [https://www.ebi.ac.uk/pdbsum/4r7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r7b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8DPI4_STRR6 Q8DPI4_STRR6] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
LicA plays a key role in the cell-wall phosphorylcholine biosynthesis of Streptococcus pneumonia. Here we determined the crystal structures of apo-form LicA at 1.94 A and two complex forms LicA-choline and LicA-AMP-MES, at 2.01 and 1.45 A resolution, respectively. The overall structure adopts a canonical protein kinase-like fold, with the active site located in the crevice of the N- and C-terminal domains. The three structures present distinct poses of the active site, which undergoes an open-closed-open conformational change upon substrate binding and product release. The structure analyses combined with mutageneses and enzymatic assays enabled us to figure out the key residues for the choline kinase activity of LicA. In addition, structural comparison revealed the loop between helices alpha7 and alpha8 might modulate the substrate specificity and catalytic activity. These findings shed light on the structure and mechanism of the prokaryotic choline kinase LicA, and might direct the rational design of novel anti-pneumococcal drugs. | |||
Structural and enzymatic characterization of the choline kinase LicA from Streptococcus pneumoniae.,Wang L, Jiang YL, Zhang JR, Zhou CZ, Chen Y PLoS One. 2015 Mar 17;10(3):e0120467. doi: 10.1371/journal.pone.0120467., eCollection 2015. PMID:25781969<ref>PMID:25781969</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4r7b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Choline kinase 3D structures|Choline kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus pneumoniae]] | |||
[[Category: Chen YX]] | |||
[[Category: Jiang YL]] | |||
[[Category: Wang L]] | |||
[[Category: Zhou CZ]] | |||
Latest revision as of 18:12, 8 November 2023
Crystal structure of pneumococcal LicA in complex with cholineCrystal structure of pneumococcal LicA in complex with choline
Structural highlights
FunctionPublication Abstract from PubMedLicA plays a key role in the cell-wall phosphorylcholine biosynthesis of Streptococcus pneumonia. Here we determined the crystal structures of apo-form LicA at 1.94 A and two complex forms LicA-choline and LicA-AMP-MES, at 2.01 and 1.45 A resolution, respectively. The overall structure adopts a canonical protein kinase-like fold, with the active site located in the crevice of the N- and C-terminal domains. The three structures present distinct poses of the active site, which undergoes an open-closed-open conformational change upon substrate binding and product release. The structure analyses combined with mutageneses and enzymatic assays enabled us to figure out the key residues for the choline kinase activity of LicA. In addition, structural comparison revealed the loop between helices alpha7 and alpha8 might modulate the substrate specificity and catalytic activity. These findings shed light on the structure and mechanism of the prokaryotic choline kinase LicA, and might direct the rational design of novel anti-pneumococcal drugs. Structural and enzymatic characterization of the choline kinase LicA from Streptococcus pneumoniae.,Wang L, Jiang YL, Zhang JR, Zhou CZ, Chen Y PLoS One. 2015 Mar 17;10(3):e0120467. doi: 10.1371/journal.pone.0120467., eCollection 2015. PMID:25781969[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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