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1knx

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1knx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knx OCA], [http://www.ebi.ac.uk/pdbsum/1knx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1knx RCSB]</span>
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Revision as of 18:51, 30 March 2008


PDB ID 1knx

Drag the structure with the mouse to rotate
, resolution 2.50Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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