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2fpr

From Proteopedia

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[[Image:2fpr.jpg|left|200px]]
 
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{{Structure
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==Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.==
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|PDB= 2fpr |SIZE=350|CAPTION= <scene name='initialview01'>2fpr</scene>, resolution 1.70&Aring;
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<StructureSection load='2fpr' size='340' side='right'caption='[[2fpr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2fpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FPR FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </span>
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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]] 1.7&#8491;</td></tr>
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|GENE= hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [https://pdbe.org/2fpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [https://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpr ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2fps|2FPS]], [[2fpu|2FPU]], [[2fpw|2FPW]], [[2fpx|2FPX]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HIS7_ECO57 HIS7_ECO57]
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== Evolutionary Conservation ==
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'''Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/2fpr_consurf.spt"</scriptWhenChecked>
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HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. HisB-N forms dimers in the crystal and in solution. The structure shows the presence of a structural Zn(2+) ion stabilizing the conformation of an extended loop. Two metal binding sites were also identified in the active site. Their presence was further confirmed by isothermal titration calorimetry. HisB-N is active in the presence of Mg(2+), Mn(2+), Co(2+), or Zn(2+), but Ca(2+) has an inhibitory effect. We have determined structures of several intermediate states corresponding to snapshots along the reaction pathway, including that of the phosphoaspartate intermediate. A catalytic mechanism, different from that described for other HAD enzymes, is proposed requiring the presence of the second metal ion not found in the active sites of previously characterized HAD enzymes, to complete the second half-reaction. The proposed mechanism is reminiscent of two-Mg(2+) ion catalysis utilized by DNA and RNA polymerases and many nucleases. The structure also provides an explanation for the inhibitory effect of Ca(2+).
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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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==About this Structure==
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</jmolCheckbox>
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2FPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA].
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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=2fpr ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway., Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M, J Biol Chem. 2006 Dec 8;281(49):37930-41. Epub 2006 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16966333 16966333]
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli O157:H7]]
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[[Category: Histidinol-phosphatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cygler M]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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[[Category: Matte A]]
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[[Category: Cygler, M]]
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[[Category: Rangarajan ES]]
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[[Category: Matte, A.]]
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[[Category: Rangarajan, E S.]]
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[[Category: bacterial structure genomic]]
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[[Category: bifunctional enzyme.]]
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[[Category: bsgi]]
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[[Category: hisb]]
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[[Category: histidinola phosphate phosphatase]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:06:08 2008''
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Current revision

Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.

PDB ID 2fpr

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