1tuy

<table><tr><td colspan='2'>[[1tuy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_1825 Dsm 1825]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TUY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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;'>[[1tuu|1tuu]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACKA, ACK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2210 DSM 1825])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate_kinase Acetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.1 2.7.2.1] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuy OCA], [http://pdbe.org/1tuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tuy RCSB], [http://www.ebi.ac.uk/pdbsum/1tuy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tuy ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ACKA_METTE ACKA_METTE]] Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Can also phosphorylate propionate, but has very low activity toward butyrate.<ref>PMID:15774882</ref>

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== Publication Abstract from PubMed ==

Acetate kinase catalyzes transfer of the gamma-phosphate of ATP to acetate. The only crystal structure reported for acetate kinase is the homodimeric enzyme from Methanosarcina thermophila containing ADP and sulfate in the active site (Buss, K. A., Cooper, D. C., Ingram-Smith, C., Ferry, J. G., Sanders, D. A., and Hasson, M. S. (2001) J. Bacteriol. 193, 680-686). Here we report two new crystal structure of the M. thermophila enzyme in the presence of substrate and transition state analogs. The enzyme co-crystallized with the ATP analog adenosine 5'-[gamma-thio]triphosphate contained AMP adjacent to thiopyrophosphate in the active site cleft of monomer B. The enzyme co-crystallized with ADP, acetate, Al(3+), and F(-) contained a linear array of ADP-AlF(3)-acetate in the active site cleft of monomer B. Together, the structures clarify the substrate binding sites and support a direct in-line transfer mechanism in which AlF(3) mimics the meta-phosphate transition state. Monomers A of both structures contained ADP and sulfate, and the active site clefts were closed less than in monomers B, suggesting that domain movement contributes to catalysis. The finding that His(180) was in close proximity to AlF(3) is consistent with a role for stabilization of the meta-phosphate that is in agreement with a previous report indicating that this residue is essential for catalysis. Residue Arg(241) was also found adjacent to AlF(3), consistent with a role for stabilization of the transition state. Kinetic analyses of Arg(241) and Arg(91) replacement variants indicated that these residues are essential for catalysis and also indicated a role in binding acetate.

Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.,Gorrell A, Lawrence SH, Ferry JG J Biol Chem. 2005 Mar 18;280(11):10731-42. Epub 2005 Jan 12. PMID:15647264<ref>PMID:15647264</ref>

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

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<div class="pdbe-citations 1tuy" style="background-color:#fffaf0;"></div>

[[Category: Acetate kinase]]

[[Category: Dsm 1825]]

[[Category: Ferry, J G]]

[[Category: Gorrell, A]]

[[Category: Lawrence, S H]]

[[Category: Alf3 and acetate]]

[[Category: Transferase]]