5cc8

<table><tr><td colspan='2'>[[5cc8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii_6013150 Acinetobacter baumannii 6013150]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CC8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CC8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiamine-phosphate_kinase Thiamine-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.16 2.7.4.16] </span></td></tr>

<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=5cc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cc8 OCA], [http://pdbe.org/5cc8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cc8 RCSB], [http://www.ebi.ac.uk/pdbsum/5cc8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cc8 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/F5HTN4_ACIBA F5HTN4_ACIBA]] Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.[HAMAP-Rule:MF_02128]

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== 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>

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== References ==

<references/>

[[Category: Thiamine-phosphate kinase]]

[[Category: Structural genomic]]

[[Category: Ssgcid]]

[[Category: Transferase]]