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[[Image:1g99.gif|left|200px]]


{{Structure
==AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA==
|PDB= 1g99 |SIZE=350|CAPTION= <scene name='initialview01'>1g99</scene>, resolution 2.5&Aring;
<StructureSection load='1g99' size='340' side='right'caption='[[1g99]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1g99]] 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=1G99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G99 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]] 2.5&#8491;</td></tr>
|GENE= 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=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=1g99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g99 OCA], [https://pdbe.org/1g99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g99 RCSB], [https://www.ebi.ac.uk/pdbsum/1g99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g99 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g99 OCA], [http://www.ebi.ac.uk/pdbsum/1g99 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g99 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 ==
'''AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA'''
[[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/g9/1g99_consurf.spt"</scriptWhenChecked>
Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP through crystallography. As we previously predicted, acetate kinase contains a core fold that is topologically identical to that of the ADP-binding domains of glycerol kinase, hexokinase, the 70-kDa heat shock cognate (Hsc70), and actin. Numerous charged active-site residues are conserved within acetate kinases, but few are conserved within the phosphotransferase superfamily. The identity of the points of insertion of polypeptide segments into the core fold of the superfamily members indicates that the insertions existed in the common ancestor of the phosphotransferases. Another remarkable shared feature is the unusual, epsilon conformation of the residue that directly precedes a conserved glycine residue (Gly-331 in acetate kinase) that binds the alpha-phosphate of ADP. Structural, biochemical, and geochemical considerations indicate that an acetate kinase may be the ancestral enzyme of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1G99 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=1G99 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=1g99 ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases., Buss KA, Cooper DR, Ingram-Smith C, Ferry JG, Sanders DA, Hasson MS, J Bacteriol. 2001 Jan;183(2):680-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11133963 11133963]
<references/>
[[Category: Acetate kinase]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanosarcina thermophila]]
[[Category: Methanosarcina thermophila]]
[[Category: Single protein]]
[[Category: Buss KA]]
[[Category: Buss, K A.]]
[[Category: Cooper DR]]
[[Category: Cooper, D R.]]
[[Category: Ferry JG]]
[[Category: Ferry, J G.]]
[[Category: Hasson MS]]
[[Category: Hasson, M S.]]
[[Category: Ingram-Smith C]]
[[Category: Ingram-Smith, C.]]
[[Category: Sanders DA]]
[[Category: Sanders, D A.]]
[[Category: actin) superfamily]]
[[Category: alpha/beta]]
[[Category: askha (acetate and sugar kinase]]
[[Category: conserved epsilon conformation]]
[[Category: hsc70]]
[[Category: two similar domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:20 2008''

Latest revision as of 10:24, 7 February 2024

AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILAAN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA

Structural highlights

1g99 is a 2 chain structure with sequence from Methanosarcina thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG. Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase. J Bacteriol. 2005 Apr;187(7):2386-94. PMID:15774882 doi:http://dx.doi.org/10.1128/JB.187.7.2386-2394.2005

1g99, resolution 2.50Å

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