5cc8: Difference between revisions

Line 8:

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cc8 OCA], [https://pdbe.org/5cc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cc8 RCSB], [https://www.ebi.ac.uk/pdbsum/5cc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cc8 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen A. baumanii in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.

Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.,Sullivan AH, Dranow DM, Horanyi PS, Lorimer DD, Edwards TE, Abendroth J Sci Rep. 2019 Mar 13;9(1):4392. doi: 10.1038/s41598-019-40558-x. PMID:30867460<ref>PMID:30867460</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Acinetobacter baumannii 6013150]]

[[Category: Large Structures]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cc8 OCA], [https://pdbe.org/5cc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cc8 RCSB], [https://www.ebi.ac.uk/pdbsum/5cc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cc8 ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen A. baumanii in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.
+Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.,Sullivan AH, Dranow DM, Horanyi PS, Lorimer DD, Edwards TE, Abendroth J Sci Rep. 2019 Mar 13;9(1):4392. doi: 10.1038/s41598-019-40558-x. PMID:30867460<ref>PMID:30867460</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5cc8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Acinetobacter baumannii 6013150]]
 [[Category: Large Structures]]