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4r78

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==Crystal structure of LicA in complex with AMP==
==Crystal structure of LicA in complex with AMP==
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<StructureSection load='4r78' size='340' side='right' caption='[[4r78]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='4r78' size='340' side='right'caption='[[4r78]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4r78]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R78 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4r78]] is a 1 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=4R78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R78 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r77|4r77]], [[4r7b|4r7b]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Choline_kinase Choline kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.32 2.7.1.32] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r78 OCA], [https://pdbe.org/4r78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r78 RCSB], [https://www.ebi.ac.uk/pdbsum/4r78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r78 ProSAT]</span></td></tr>
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<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=4r78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r78 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r78 RCSB], [http://www.ebi.ac.uk/pdbsum/4r78 PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8DPI4_STRR6 Q8DPI4_STRR6]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Choline kinase 3D structures|Choline kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Choline kinase]]
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[[Category: Large Structures]]
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[[Category: Chen, Y X]]
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[[Category: Streptococcus pneumoniae]]
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[[Category: Jiang, Y L]]
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[[Category: Chen YX]]
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[[Category: Wang, L]]
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[[Category: Jiang YL]]
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[[Category: Zhou, C Z]]
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[[Category: Wang L]]
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[[Category: Protein kinase-like fold]]
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[[Category: Zhou CZ]]
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[[Category: Transferase]]
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Current revision

Crystal structure of LicA in complex with AMP

PDB ID 4r78

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