1ko7
From Proteopedia
(New page: 200px<br /><applet load="1ko7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ko7, resolution 1.95Å" /> '''X-ray structure of t...) |
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| - | [[Image:1ko7.gif|left|200px]]<br /><applet load="1ko7" size=" | + | [[Image:1ko7.gif|left|200px]]<br /><applet load="1ko7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ko7, resolution 1.95Å" /> | caption="1ko7, resolution 1.95Å" /> | ||
'''X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution'''<br /> | '''X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The histidine containing phospho carrier protein (HPr) kinase/phosphatase | + | The histidine containing phospho carrier protein (HPr) kinase/phosphatase is involved in carbon catabolite repression, mainly in Gram-positive bacteria. It is a bifunctional enzyme that phosphorylates Ser-46-HPr in an ATP-dependent reaction and dephosphorylates P-Ser-46-HPr. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller. The N-terminal domain has a betaalphabeta fold similar to a segment from enzyme I of the sugar phosphotransferase system and to the uridyl-binding portion of MurF; it is structurally organized in three dimeric modules exposed to form the propeller blades. Two unexpected phosphate ions associated with highly conserved residues were found in the N-terminal dimeric interface. The C-terminal kinase domain is similar to that of the Lactobacillus casei enzyme and is assembled in six copies to form the compact central hub of the propeller. Beyond previously reported similarity with adenylate kinase, we suggest evolutionary relationship with phosphoenolpyruvate carboxykinase. In addition to a phosphate ion in the phosphate-binding loop of the kinase domain, we have identified a second phosphate-binding site that, by comparison with adenylate kinases, we believe accommodates a product/substrate phosphate, normally covalently linked to Ser-46 of HPr. Thus, we propose that our structure represents a product/substrate mimic of the kinase/phosphatase reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1KO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_xylosus Staphylococcus xylosus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1KO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_xylosus Staphylococcus xylosus] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KO7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hengstenberg, W.]] | [[Category: Hengstenberg, W.]] | ||
[[Category: Koch, B.]] | [[Category: Koch, B.]] | ||
| - | [[Category: Marquez, J | + | [[Category: Marquez, J A.]] |
[[Category: Nessler, S.]] | [[Category: Nessler, S.]] | ||
[[Category: Scheffzek, K.]] | [[Category: Scheffzek, K.]] | ||
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[[Category: substrate]] | [[Category: substrate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:17 2008'' |
Revision as of 11:36, 21 February 2008
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X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution
Overview
The histidine containing phospho carrier protein (HPr) kinase/phosphatase is involved in carbon catabolite repression, mainly in Gram-positive bacteria. It is a bifunctional enzyme that phosphorylates Ser-46-HPr in an ATP-dependent reaction and dephosphorylates P-Ser-46-HPr. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller. The N-terminal domain has a betaalphabeta fold similar to a segment from enzyme I of the sugar phosphotransferase system and to the uridyl-binding portion of MurF; it is structurally organized in three dimeric modules exposed to form the propeller blades. Two unexpected phosphate ions associated with highly conserved residues were found in the N-terminal dimeric interface. The C-terminal kinase domain is similar to that of the Lactobacillus casei enzyme and is assembled in six copies to form the compact central hub of the propeller. Beyond previously reported similarity with adenylate kinase, we suggest evolutionary relationship with phosphoenolpyruvate carboxykinase. In addition to a phosphate ion in the phosphate-binding loop of the kinase domain, we have identified a second phosphate-binding site that, by comparison with adenylate kinases, we believe accommodates a product/substrate phosphate, normally covalently linked to Ser-46 of HPr. Thus, we propose that our structure represents a product/substrate mimic of the kinase/phosphatase reaction.
About this Structure
1KO7 is a Single protein structure of sequence from Staphylococcus xylosus with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions., Marquez JA, Hasenbein S, Koch B, Fieulaine S, Nessler S, Russell RB, Hengstenberg W, Scheffzek K, Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3458-63. PMID:11904409
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