1knx
From Proteopedia
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[[Image:1knx.gif|left|200px]] | [[Image:1knx.gif|left|200px]] | ||
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'''HPr kinase/phosphatase from Mycoplasma pneumoniae''' | '''HPr kinase/phosphatase from Mycoplasma pneumoniae''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Allen, G S.]] | [[Category: Allen, G S.]] | ||
| - | [[Category: | + | [[Category: Catabolite repression]] |
| - | [[Category: | + | [[Category: Hpr kinase]] |
| - | [[Category: | + | [[Category: Hpr kinase/phosphatase]] |
| - | [[Category: | + | [[Category: Hprk/p]] |
| - | [[Category: | + | [[Category: Kinase]] |
| - | [[Category: | + | [[Category: P-loop]] |
| - | [[Category: | + | [[Category: Phosphatase]] |
| - | [[Category: | + | [[Category: Walker a box]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:57, 2 May 2008
HPr kinase/phosphatase from Mycoplasma pneumoniae
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.
About this Structure
1KNX is a Single protein structure of sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA.
Reference
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 Fri May 2 22:57:54 2008
