2hw4

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[[Image:2hw4.gif|left|200px]]
 
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{{Structure
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==Crystal structure of human phosphohistidine phosphatase==
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|PDB= 2hw4 |SIZE=350|CAPTION= <scene name='initialview01'>2hw4</scene>, resolution 1.90&Aring;
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<StructureSection load='2hw4' size='340' side='right'caption='[[2hw4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
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<table><tr><td colspan='2'>[[2hw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HW4 FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.9&#8491;</td></tr>
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|GENE= PHPT1, PHP14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
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}}
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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=2hw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hw4 OCA], [https://pdbe.org/2hw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hw4 RCSB], [https://www.ebi.ac.uk/pdbsum/2hw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hw4 ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of human phosphohistidine phosphatase'''
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== Function ==
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[https://www.uniprot.org/uniprot/PHP14_HUMAN PHP14_HUMAN] Exhibits phosphohistidine phosphatase activity.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. The structure of phosphohistidine phosphatase (PHPT1), the first identified eukaryotic-protein histidine phosphatase, has been determined to a resolution of 1.9A using multiple-wavelength anomalous dispersion methods. This enzyme can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues. Histidine 53 is proposed to play a major role in histidine dephosphorylation based on these observations and previous mutational studies. Models of peptide binding are discussed to suggest possible mechanisms for substrate recognition.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/2hw4_consurf.spt"</scriptWhenChecked>
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2HW4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HW4 OCA].
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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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==Reference==
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</jmolCheckbox>
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First structure of a eukaryotic phosphohistidine phosphatase., Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Hallberg BM, J Biol Chem. 2006 Nov 10;281(45):33830-4. Epub 2006 Sep 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16990267 16990267]
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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=2hw4 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C.]]
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[[Category: Arrowsmith C]]
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[[Category: Berg, S Van Den.]]
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[[Category: Berglund H]]
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[[Category: Berglund, H.]]
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[[Category: Busam RD]]
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[[Category: Busam, R D.]]
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[[Category: Collins R]]
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[[Category: Collins, R.]]
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[[Category: Edwards A]]
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[[Category: Edwards, A.]]
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[[Category: Ehn M]]
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[[Category: Ehn, M.]]
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[[Category: Flodin S]]
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[[Category: Flodin, S.]]
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[[Category: Flores A]]
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[[Category: Flores, A.]]
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[[Category: Graslund S]]
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[[Category: Graslund, S.]]
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[[Category: Hallberg BM]]
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[[Category: Hallberg, B M.]]
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[[Category: Hammarstrom M]]
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[[Category: Hammarstrom, M.]]
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[[Category: Hogbom M]]
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[[Category: Hogbom, M.]]
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[[Category: Holmberg Schiavone L]]
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[[Category: Kotenyova, T.]]
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[[Category: Kotenyova T]]
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[[Category: Nilsson-Ehle, P.]]
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[[Category: Nilsson-Ehle P]]
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[[Category: Nordlund, P.]]
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[[Category: Nordlund P]]
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[[Category: Nyman, T.]]
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[[Category: Nyman T]]
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[[Category: Ogg, D.]]
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[[Category: Ogg D]]
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[[Category: Persson, C.]]
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[[Category: Persson C]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Stenmark P]]
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[[Category: Schiavone, L Holmberg.]]
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[[Category: Sundstrom M]]
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[[Category: Stenmark, P.]]
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[[Category: Thorsell AG]]
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[[Category: Sundstrom, M.]]
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[[Category: Uppenberg J]]
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[[Category: Thorsell, A G.]]
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[[Category: Van Den Berg S]]
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[[Category: Uppenberg, J.]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J.]]
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[[Category: FMT]]
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[[Category: human]]
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[[Category: phosphatase]]
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[[Category: phosphohistidine]]
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[[Category: phpt1]]
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[[Category: sgc]]
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[[Category: structural genomic]]
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[[Category: structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:22:18 2008''
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Current revision

Crystal structure of human phosphohistidine phosphatase

PDB ID 2hw4

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