1knx: Difference between revisions

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<StructureSection load='1knx' size='340' side='right'caption='[[1knx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1knx' size='340' side='right'caption='[[1knx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1knx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"filterable_agent_of_primary_atypical_pneumonia"_eaton_et_al._1944 "filterable agent of primary atypical pneumonia" eaton et al. 1944]. 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>
<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>
</td></tr><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>
</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>
<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>
</table>
</table>
== Function ==
== Function ==
[[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]  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12589763</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1knx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Filterable agent of primary atypical pneumonia eaton et al. 1944]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Allen, G S]]
[[Category: Mycoplasma pneumoniae]]
[[Category: Catabolite repression]]
[[Category: Allen GS]]
[[Category: Hpr kinase]]
[[Category: Hpr kinase/phosphatase]]
[[Category: Hprk/p]]
[[Category: Kinase]]
[[Category: P-loop]]
[[Category: Phosphatase]]
[[Category: Transferase-hydrolase complex]]
[[Category: Walker a box]]

Latest revision as of 10:26, 14 February 2024

HPr kinase/phosphatase from Mycoplasma pneumoniaeHPr kinase/phosphatase from Mycoplasma pneumoniae

Structural highlights

1knx is a 6 chain structure with sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1knx, resolution 2.50Å

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OCA
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