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1knx

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(New page: 200px<br /><applet load="1knx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1knx, resolution 2.50&Aring;" /> '''HPr kinase/phosphata...)
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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;" />
 
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'''HPr kinase/phosphatase from Mycoplasma pneumoniae'''<br />
 
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==Overview==
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==HPr kinase/phosphatase from Mycoplasma pneumoniae==
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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.
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<StructureSection load='1knx' size='340' side='right'caption='[[1knx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1KNX 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].
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</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>
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<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>
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==Reference==
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</table>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12589763 12589763]
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1knx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mycoplasma pneumoniae]]
[[Category: Mycoplasma pneumoniae]]
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[[Category: Single protein]]
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[[Category: Allen GS]]
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[[Category: Allen, G.S.]]
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[[Category: catabolite repression]]
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[[Category: hpr kinase]]
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[[Category: hpr kinase/phosphatase]]
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[[Category: hprk/p]]
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[[Category: kinase]]
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[[Category: p-loop]]
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[[Category: phosphatase]]
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[[Category: walker a box]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:27:03 2007''
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Current revision

HPr kinase/phosphatase from Mycoplasma pneumoniae

PDB ID 1knx

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