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| - | [[Image:1tuu.gif|left|200px]] | |
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| - | {{Structure
| + | ==Acetate Kinase crystallized with ATPgS== |
| - | |PDB= 1tuu |SIZE=350|CAPTION= <scene name='initialview01'>1tuu</scene>, resolution 2.50Å
| + | <StructureSection load='1tuu' size='340' side='right'caption='[[1tuu]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PIS:TRIHYDROGEN+THIODIPHOSPHATE'>PIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | <table><tr><td colspan='2'>[[1tuu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUU FirstGlance]. <br> |
| - | |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | |GENE= ACKA, ACK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2210 Methanosarcina thermophila])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PIS:TRIHYDROGEN+THIODIPHOSPHATE'>PIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuu OCA], [https://pdbe.org/1tuu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tuu RCSB], [https://www.ebi.ac.uk/pdbsum/1tuu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tuu ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuu OCA], [http://www.ebi.ac.uk/pdbsum/1tuu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tuu RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://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> |
| - | | + | == Evolutionary Conservation == |
| - | '''Acetate Kinase crystallized with ATPgS'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | | + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tu/1tuu_consurf.spt"</scriptWhenChecked> |
| - | 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.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 1TUU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUU OCA].
| + | </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=1tuu ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference== | + | == References == |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15647264 15647264]
| + | <references/> |
| - | [[Category: Acetate kinase]] | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Methanosarcina thermophila]] | | [[Category: Methanosarcina thermophila]] |
| - | [[Category: Single protein]]
| + | [[Category: Ferry JG]] |
| - | [[Category: Ferry, J G.]] | + | [[Category: Gorrell A]] |
| - | [[Category: Gorrell, A.]] | + | [[Category: Lawrence SH]] |
| - | [[Category: Lawrence, S H.]] | + | |
| - | [[Category: alpha/beta]]
| + | |
| - | [[Category: askha (acetate and sugar kinase]]
| + | |
| - | [[Category: hsc70 actin) superfamily]]
| + | |
| - | [[Category: two similar domain]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:23 2008''
| + | |
