3c9r
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_3c9r| PDB=3c9r | SCENE= }} | ||
| - | ===AaThiL complexed with ATP=== | ||
| - | {{ABSTRACT_PUBMED_18311927}} | ||
| - | == | + | ==AaThiL complexed with ATP== |
| - | [[3c9r]] is a 2 chain structure with sequence from [ | + | <StructureSection load='3c9r' size='340' side='right'caption='[[3c9r]], [[Resolution|resolution]] 2.30Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3c9r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c9s|3c9s]], [[3c9t|3c9t]], [[3c9u|3c9u]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thiL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiamine-phosphate_kinase Thiamine-phosphate kinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3c9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9r OCA], [https://pdbe.org/3c9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9r RCSB], [https://www.ebi.ac.uk/pdbsum/3c9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/THIL_AQUAE THIL_AQUAE]] Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.<ref>PMID:18311927</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9r_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3c9r ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thiamin monophosphate kinase (ThiL) catalyzes the ATP-dependent phosphorylation of thiamin monophosphate (TMP) to form thiamin pyrophosphate (TPP), the active form of vitamin B 1. ThiL is a member of a small ATP binding superfamily that also includes the purine biosynthetic enzymes, PurM and PurL, NiFe hydrogenase maturation protein, HypE, and selenophosphate synthase, SelD. The latter four enzymes are believed to utilize phosphorylated intermediates during catalysis. To understand the mechanism of ThiL and its relationship to the other superfamily members, we determined the structure of Aquifex aeolicus ThiL (AaThiL) with nonhydrolyzable AMP-PCP and TMP, and also with the products of the reaction, ADP and TPP. The results suggest that AaThiL utilizes a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate. The structure of ThiL is compared to those of PurM, PurL, and HypE, and the ATP binding site is compared to that of PurL, for which nucleotide complexes are available. | ||
| - | + | Structural studies of thiamin monophosphate kinase in complex with substrates and products(,).,McCulloch KM, Kinsland C, Begley TP, Ealick SE Biochemistry. 2008 Mar 25;47(12):3810-21. Epub 2008 Mar 1. PMID:18311927<ref>PMID:18311927</ref> | |
| - | <ref | + | |
| - | [[Category: Aquifex aeolicus]] | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 3c9r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aquifex aeolicus huber and stetter 2001]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thiamine-phosphate kinase]] | [[Category: Thiamine-phosphate kinase]] | ||
| - | [[Category: Begley, T P | + | [[Category: Begley, T P]] |
| - | [[Category: Ealick, S E | + | [[Category: Ealick, S E]] |
| - | [[Category: Kinsland, C | + | [[Category: Kinsland, C]] |
| - | [[Category: McCulloch, K M | + | [[Category: McCulloch, K M]] |
[[Category: Alpha-beta structure]] | [[Category: Alpha-beta structure]] | ||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Current revision
AaThiL complexed with ATP
| |||||||||||
