1g99
From Proteopedia
(New page: 200px<br /><applet load="1g99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g99, resolution 2.5Å" /> '''AN ANCIENT ENZYME: AC...) |
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| - | [[Image:1g99.gif|left|200px]]<br /><applet load="1g99" size=" | + | [[Image:1g99.gif|left|200px]]<br /><applet load="1g99" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g99, resolution 2.5Å" /> | caption="1g99, resolution 2.5Å" /> | ||
'''AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA'''<br /> | '''AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1G99 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 and ADP 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:// | + | 1G99 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1G99 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanosarcina thermophila]] | [[Category: Methanosarcina thermophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buss, K | + | [[Category: Buss, K A.]] |
| - | [[Category: Cooper, D | + | [[Category: Cooper, D R.]] |
| - | [[Category: Ferry, J | + | [[Category: Ferry, J G.]] |
| - | [[Category: Hasson, M | + | [[Category: Hasson, M S.]] |
[[Category: Ingram-Smith, C.]] | [[Category: Ingram-Smith, C.]] | ||
| - | [[Category: Sanders, D | + | [[Category: Sanders, D A.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: hsc70]] | [[Category: hsc70]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:32 2008'' |
Revision as of 10:47, 21 February 2008
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AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA
Overview
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.
About this Structure
1G99 is a Single protein structure of sequence from Methanosarcina thermophila with and as ligands. Active as Acetate kinase, with EC number 2.7.2.1 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:47:32 2008
Categories: Acetate kinase | Methanosarcina thermophila | Single protein | Buss, K A. | Cooper, D R. | Ferry, J G. | Hasson, M S. | Ingram-Smith, C. | Sanders, D A. | ADP | SO4 | Actin) superfamily; conserved epsilon conformation; two similar domains | Alpha/beta; askha (acetate and sugar kinases | Hsc70
