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1tuy

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(New page: 200px<br /><applet load="1tuy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tuy, resolution 3.00&Aring;" /> '''Acetate Kinase compl...)
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[[Image:1tuy.gif|left|200px]]<br /><applet load="1tuy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tuy, resolution 3.00&Aring;" />
 
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'''Acetate Kinase complexed with ADP, AlF3 and acetate'''<br />
 
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==Overview==
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==Acetate Kinase complexed with ADP, AlF3 and acetate==
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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.
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<StructureSection load='1tuy' size='340' side='right'caption='[[1tuy]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1tuy]] 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=1TUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUY FirstGlance]. <br>
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1TUY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila] with SO4, ADP, AF3 and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TUY OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<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>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuy OCA], [https://pdbe.org/1tuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tuy RCSB], [https://www.ebi.ac.uk/pdbsum/1tuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tuy ProSAT]</span></td></tr>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15647264 15647264]
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</table>
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[[Category: Acetate kinase]]
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tu/1tuy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tuy ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanosarcina thermophila]]
[[Category: Methanosarcina thermophila]]
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[[Category: Single protein]]
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[[Category: Ferry JG]]
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[[Category: Ferry, J.G.]]
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[[Category: Gorrell A]]
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[[Category: Gorrell, A.]]
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[[Category: Lawrence SH]]
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[[Category: Lawrence, S.H.]]
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[[Category: ACY]]
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[[Category: ADP]]
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[[Category: AF3]]
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[[Category: SO4]]
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[[Category: actin) superfamily]]
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[[Category: alf3 and acetate]]
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[[Category: alpha/beta]]
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[[Category: askha (acetate and sugar kinases]]
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[[Category: hsc70]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:36:52 2007''
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Current revision

Acetate Kinase complexed with ADP, AlF3 and acetate

PDB ID 1tuy

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