1g99: Difference between revisions

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<StructureSection load='1g99' size='340' side='right'caption='[[1g99]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1g99' size='340' side='right'caption='[[1g99]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g99]] 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=1G99 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1G99 FirstGlance]. <br>
<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>
</td></tr><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>
</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2210 DSM 1825])</td></tr>
<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>
<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'>[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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1g99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g99 OCA], [http://pdbe.org/1g99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g99 RCSB], [http://www.ebi.ac.uk/pdbsum/1g99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g99 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1g99 ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:11133963<ref>PMID:11133963</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1g99" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acetate kinase]]
[[Category: Dsm 1825]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Buss, K A]]
[[Category: Methanosarcina thermophila]]
[[Category: Cooper, D R]]
[[Category: Buss KA]]
[[Category: Ferry, J G]]
[[Category: Cooper DR]]
[[Category: Hasson, M S]]
[[Category: Ferry JG]]
[[Category: Ingram-Smith, C]]
[[Category: Hasson MS]]
[[Category: Sanders, D A]]
[[Category: Ingram-Smith C]]
[[Category: Alpha/beta]]
[[Category: Sanders DA]]
[[Category: Conserved epsilon conformation]]
[[Category: Hsc70]]
[[Category: Transferase]]
[[Category: Two similar domain]]

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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