1knx: Difference between revisions

Revision as of 14:36, 21 February 2008

HPr kinase/phosphatase from Mycoplasma pneumoniae

OverviewOverview

HPr kinase/phosphatase (HPrK/P) modifies serine 46 of histidine-containing protein (HPr), the phosphorylation state of which is the control point of carbon catabolite repression in low G+C Gram-positive bacteria. To understand the structural mechanism by which HPrK/P carries out its dual, competing activities we determined the structure of full length HPrK/P from Mycoplasma pneumoniae (PD8 ID, 1KNX) to 2.5A resolution. The enzyme forms a homo-hexamer with each subunit containing two domains connected by a short loop. The C-terminal domain contains the well-described P-loop (Walker A box) ATP binding motif and takes a fold similar to phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as recently described in other HPrK/P structures. As expected, the C-terminal domain is very similar to the C-terminal fragment of Lactobacillus casei HPrK/P and the C-terminal domain of Staphylococcus xylosus HPrK/P; the N-terminal domain is very similar to the N-terminal domain of S.xylosus HPrK/P. Unexpectedly, the N-terminal domain resembles UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase (MurE), yet the function of this domain is unclear. We discuss these observations as well as the structural significance of mutations in the P-loop and HPrK/P family sequence motif.

About this StructureAbout this Structure

1KNX is a Single protein structure of sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae., Allen GS, Steinhauer K, Hillen W, Stulke J, Brennan RG, J Mol Biol. 2003 Feb 28;326(4):1203-17. PMID:12589763

Page seeded by OCA on Thu Feb 21 13:36:06 2008

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OCA

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-[[Image:1knx.gif|left|200px]]<br /><applet load="1knx" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1knx, resolution 2.50&Aring;" />
 '''HPr kinase/phosphatase from Mycoplasma pneumoniae'''<br />
 ==Overview==
-HPr kinase/phosphatase (HPrK/P) modifies serine 46 of histidine-containing, protein (HPr), the phosphorylation state of which is the control point of, carbon catabolite repression in low G+C Gram-positive bacteria. To, understand the structural mechanism by which HPrK/P carries out its dual, competing activities we determined the structure of full length HPrK/P, from Mycoplasma pneumoniae (PD8 ID, 1KNX) to 2.5A resolution. The enzyme, forms a homo-hexamer with each subunit containing two domains connected by, a short loop. The C-terminal domain contains the well-described P-loop, (Walker A box) ATP binding motif and takes a fold similar to, phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as, recently described in other HPrK/P structures. As expected, the C-terminal, domain is very similar to the C-terminal fragment of Lactobacillus casei, HPrK/P and the C-terminal domain of Staphylococcus xylosus HPrK/P; the, N-terminal domain is very similar to the N-terminal domain of S.xylosus, HPrK/P. Unexpectedly, the N-terminal domain resembles, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase, (MurE), yet the function of this domain is unclear. We discuss these, observations as well as the structural significance of mutations in the, P-loop and HPrK/P family sequence motif.
+HPr kinase/phosphatase (HPrK/P) modifies serine 46 of histidine-containing protein (HPr), the phosphorylation state of which is the control point of carbon catabolite repression in low G+C Gram-positive bacteria. To understand the structural mechanism by which HPrK/P carries out its dual, competing activities we determined the structure of full length HPrK/P from Mycoplasma pneumoniae (PD8 ID, 1KNX) to 2.5A resolution. The enzyme forms a homo-hexamer with each subunit containing two domains connected by a short loop. The C-terminal domain contains the well-described P-loop (Walker A box) ATP binding motif and takes a fold similar to phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as recently described in other HPrK/P structures. As expected, the C-terminal domain is very similar to the C-terminal fragment of Lactobacillus casei HPrK/P and the C-terminal domain of Staphylococcus xylosus HPrK/P; the N-terminal domain is very similar to the N-terminal domain of S.xylosus HPrK/P. Unexpectedly, the N-terminal domain resembles UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase (MurE), yet the function of this domain is unclear. We discuss these observations as well as the structural significance of mutations in the P-loop and HPrK/P family sequence motif.
 ==About this Structure==
-KNX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_pneumoniae Mycoplasma pneumoniae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KNX OCA].
+KNX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_pneumoniae Mycoplasma pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNX OCA].
 ==Reference==
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 [[Category: Mycoplasma pneumoniae]]
 [[Category: Single protein]]
-[[Category: Allen, G.S.]]
+[[Category: Allen, G S.]]
 [[Category: catabolite repression]]
 [[Category: hpr kinase]]
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 [[Category: walker a box]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:27:03 2007''
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