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[[Image:1knx.gif|left|200px]]


{{Structure
==HPr kinase/phosphatase from Mycoplasma pneumoniae==
|PDB= 1knx |SIZE=350|CAPTION= <scene name='initialview01'>1knx</scene>, resolution 2.50&Aring;
<StructureSection load='1knx' size='340' side='right'caption='[[1knx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1knx]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KNX FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1knx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knx OCA], [https://pdbe.org/1knx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1knx RCSB], [https://www.ebi.ac.uk/pdbsum/1knx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1knx ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|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>
[https://www.uniprot.org/uniprot/HPRK_MYCPN HPRK_MYCPN] Is a metabolite-sensitive enzyme that catalyzes the ATP-as well as probably the pyrophosphate-dependent phosphorylation of Ser-47 in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The regulatory role of HPrK/P in the physiology of M.pneumoniae is not known yet.[HAMAP-Rule:MF_01249]
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''HPr kinase/phosphatase from Mycoplasma pneumoniae'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1knx_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1knx ConSurf].
1KNX is a [[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].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
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:[http://www.ncbi.nlm.nih.gov/pubmed/12589763 12589763]
[[Category: Large Structures]]
[[Category: Mycoplasma pneumoniae]]
[[Category: Mycoplasma pneumoniae]]
[[Category: Single protein]]
[[Category: Allen GS]]
[[Category: Allen, G S.]]
[[Category: catabolite repression]]
[[Category: hpr kinase]]
[[Category: hpr kinase/phosphatase]]
[[Category: hprk/p]]
[[Category: kinase]]
[[Category: p-loop]]
[[Category: phosphatase]]
[[Category: walker a box]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:11 2008''

Latest revision as of 07:26, 14 February 2024

HPr kinase/phosphatase from Mycoplasma pneumoniae

1knx, resolution 2.50Å

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